Summary: ArgK protein
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ArgK protein Provide feedback
The ArgK protein acts as an ATPase enzyme and as a kinase, and phosphorylates periplasmic binding proteins involved in the LAO (lysine, arginine, ornithine)/AO transport systems.
Celis RT, Leadlay PF, Roy I, Hansen A; , J Bacteriol 1998;180:4828-4833.: Phosphorylation of the periplasmic binding protein in two transport systems for arginine incorporation in Escherichia coli K-12 is unrelated to the function of the transport system. PUBMED:9733684 EPMC:9733684
Internal database links
|Similarity to PfamA using HHSearch:||AAA ATP_bind_1 cobW GTP_EFTU SRP54 ABC_tran APS_kinase CbiA DUF258 NTPase_1 DUF87 IstB_IS21 MMR_HSR1 MobB KTI12 AAA_10 AAA_16 AAA_17 AAA_18 AAA_19 AAA_22 AAA_23 AAA_25 AAA_28 AAA_29 AAA_30 AAA_31 AAA_33|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005129
YgfD was first identified as an ATPase, ArgK, which appeared to phosphorylate the periplasmic binding proteins of the lysine, arginine, ornithine (LAO) transport system, as well as the arginine, ornithine transport system [PUBMED:2136858]. Bacterial periplasmic transport systems require the function of a specific substrate-binding protein, located in the periplasm, and several cytoplasmic membrane transport components. In Escherichia coli, the arginine-ornithine transport system requires an arginine-ornithine-binding protein and the lysine-arginine-ornithine (LAO) transport system includes a LAO-binding protein. Both periplasmic proteins were shown to be phosphorylated by ArgK [PUBMED:2136858], resulting in reduced levels of transport activity.
However, another study showed that the kinase activity of ArgK did not affect transport activity [PUBMED:9733684]. Furthermore, neither the molecular weight nor the pI of ArgK are similar to that of the protein kinase that was purified based on its activity [PUBMED:2104851]. YgfK has been identified as part of an operon that encodes enzymes converting succinate to propionate [PUBMED:18950999]. YgfD was confirmed to have GTPase activity, but no function could be assigned to it. The function of ArgK remains unclear.
This entry represents ArgK and other proteins of the ArgK family. It includes methylmalonic aciduria type A protein, which may have GTPase and ATPase activity and function as chaperone. In Caenorhabditis elegans, this protein is likely to have a role in propionyl-CoA metabolism and adenosylcobalamin synthesis [PUBMED:16843692].
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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_3540 (release 6.5)|
|Number in seed:||9|
|Number in full:||1738|
|Average length of the domain:||266.50 aa|
|Average identity of full alignment:||40 %|
|Average coverage of the sequence by the domain:||60.95 %|
|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:||11|
|Download:||download the raw HMM for this family|
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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 ArgK domain has been found. There are 12 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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