Summary: Anion-transporting ATPase
This is the Wikipedia entry entitled "Ars operon". More...
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Ars operon Edit Wikipedia article
yffb (pa3664) protein
In molecular biology, the ars operon is an operon found in several bacterial taxon. It is required for the detoxification of arsenate, arsenite, and antimonite. This system transports arsenite and antimonite out of the cell. The pump is composed of two polypeptides, the products of the arsA and arsB genes. This two-subunit enzyme produces resistance to arsenite and antimonite. Arsenate, however, must first be reduced to arsenite before it is extruded. A third gene, arsC, expands the substrate specificity to allow for arsenate pumping and resistance. ArsC is an approximately 150-residue arsenate reductase that uses reduced glutathione (GSH) to convert arsenate to arsenite with a redox active cysteine residue in the active site. ArsC forms an active quaternary complex with GSH, arsenate, and glutaredoxin 1 (Grx1). The three ligands must be present simultaneously for reduction to occur.
ArsA and ArsB
ArsA and ArsB form an anion-translocating ATPase. The ArsB protein is distinguished by its overall hydrophobic character, in keeping with its role as a membrane-associated channel. Sequence analysis reveals the presence of 13 putative transmembrane (TM) regions.
The arsC protein structure has been solved. It belongs to the thioredoxin superfamily fold which is defined by a beta-sheet core surrounded by alpha-helices. The active cysteine residue of ArsC is located in the loop between the first beta-strand and the first helix, which is also conserved in the Spx protein and its homologues.
ArsD and ArsR
ArsD is a trans-acting repressor of the arsRDABC operon that confers resistance to arsenicals and antimonials in Escherichia coli. It possesses two-pairs of vicinal cysteine residues, Cys(12)-Cys(13) and Cys(112)-Cys(113), that potentially form separate binding sites for the metalloids that trigger dissociation of ArsD from the operon. However, as a homodimer it has four vicinal cysteine pairs. The ArsD family consists of several bacterial arsenical resistance operon trans-acting repressor ArsD proteins.
ArsR is a trans-acting regulatory protein. It acts as a repressor on the arsRDABC operon when no arsenic is present in the cell. When arsenic is present in the cell ArsR will lose affinity for the operator and RNA polymerase can transcribe the arsDCAB genes. ArsD and ArsR work together to regulate the ars operon.
- Carlin A, Shi W, Dey S, Rosen BP (February 1995). "The ars operon of Escherichia coli confers arsenical and antimonial resistance". J. Bacteriol. 177 (4): 981–6. PMC 176692. PMID 7860609.
- Liu J, Rosen BP (August 1997). "Ligand interactions of the ArsC arsenate reductase". J. Biol. Chem. 272 (34): 21084–9. doi:10.1074/jbc.272.34.21084. PMID 9261111.
- Rosen BP (1990). "The plasmid-encoded arsenical resistance pump: an anion-translocating ATPase.". Res Microbiol 141 (3): 336–41. doi:10.1016/0923-2508(90)90008-e. PMID 1704144.
- Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF (November 2001). "Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme". Structure 9 (11): 1071–81. doi:10.1016/S0969-2126(01)00672-4. PMID 11709171.
- Zuber P (April 2004). "Spx-RNA polymerase interaction and global transcriptional control during oxidative stress". J. Bacteriol. 186 (7): 1911–8. doi:10.1128/jb.186.7.1911-1918.2004. PMC 374421. PMID 15028674.
- Li S, Rosen BP, Borges-Walmsley MI, Walmsley AR (July 2002). "Evidence for cooperativity between the four binding sites of dimeric ArsD, an As(III)-responsive transcriptional regulator". J. Biol. Chem. 277 (29): 25992–6002. doi:10.1074/jbc.M201619200. PMID 11980902.
Anion-transporting ATPase Provide feedback
This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.
Internal database links
|Similarity to PfamA using HHSearch:||SRP54 APS_kinase CbiA Fer4_NifH IstB_IS21 YhjQ MipZ AAA_17 AAA_18 AAA_24 AAA_31|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR025723
This entry represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase [PUBMED:1704144, PUBMED:10970874]. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell. The entry also matches some sequences from the Mrp/NBP35 ATP-binding proteins family.
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes .
The clan contains the following 198 members:6PF2K AAA AAA-ATPase_like AAA_10 AAA_11 AAA_12 AAA_13 AAA_14 AAA_15 AAA_16 AAA_17 AAA_18 AAA_19 AAA_2 AAA_21 AAA_22 AAA_23 AAA_24 AAA_25 AAA_26 AAA_27 AAA_28 AAA_29 AAA_3 AAA_30 AAA_31 AAA_32 AAA_33 AAA_34 AAA_35 AAA_4 AAA_5 AAA_6 AAA_7 AAA_8 AAA_9 AAA_PrkA ABC_ATPase ABC_tran ABC_tran_2 Adeno_IVa2 Adenylsucc_synt ADK AFG1_ATPase AIG1 APS_kinase Arch_ATPase Arf ArgK ArsA_ATPase ATP-synt_ab ATP_bind_1 ATP_bind_2 Bac_DnaA CbiA CMS1 CoaE CobA_CobO_BtuR CobU cobW CPT CTP_synth_N Cytidylate_kin Cytidylate_kin2 DAP3 DEAD DEAD_2 DLIC DNA_pack_C DNA_pack_N DNA_pol3_delta DNA_pol3_delta2 DnaB_C dNK DUF1253 DUF1611 DUF2075 DUF2478 DUF258 DUF2791 DUF2813 DUF3584 DUF463 DUF815 DUF853 DUF87 DUF927 Dynamin_N Exonuc_V_gamma FeoB_N Fer4_NifH Flavi_DEAD FTHFS FtsK_SpoIIIE G-alpha Gal-3-0_sulfotr GBP GTP_EFTU GTP_EFTU_D2 GTP_EFTU_D4 Gtr1_RagA Guanylate_kin GvpD HDA2-3 Helicase_C Helicase_C_2 Helicase_C_4 Helicase_RecD Herpes_Helicase Herpes_ori_bp Herpes_TK IIGP IPPT IPT IstB_IS21 KaiC KAP_NTPase Kinesin Kinesin-relat_1 Kinesin-related KTI12 LpxK MCM MEDS Mg_chelatase Mg_chelatase_2 MipZ Miro MMR_HSR1 MobB MukB MutS_V Myosin_head NACHT NB-ARC NOG1 NTPase_1 ParA Parvo_NS1 PAXNEB PduV-EutP PhoH PIF1 Podovirus_Gp16 Polyoma_lg_T_C Pox_A32 PPK2 PPV_E1_C PRK Rad17 Rad51 Ras RecA ResIII RHD3 RHSP RNA12 RNA_helicase RuvB_N SbcCD_C SecA_DEAD Septin Sigma54_activ_2 Sigma54_activat SKI SMC_N SNF2_N Spore_IV_A SRP54 SRPRB Sulfotransfer_1 Sulfotransfer_2 Sulfotransfer_3 Sulphotransf T2SE T4SS-DNA_transf Terminase_1 Terminase_3 Terminase_6 Terminase_GpA Thymidylate_kin TIP49 TK TniB Torsin TraG-D_C tRNA_lig_kinase TrwB_AAD_bind UPF0079 UvrD-helicase UvrD_C UvrD_C_2 Viral_helicase1 VirC1 VirE YhjQ Zeta_toxin Zot
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Curation and family details
|Seed source:||Pfam-B_1201 (release 5.2)|
|Author:||Mian N, Bateman A|
|Number in seed:||11|
|Number in full:||2686|
|Average length of the domain:||239.70 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||76.97 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ArsA_ATPase domain has been found. There are 72 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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