Summary: ZinT (YodA) periplasmic lipocalin-like zinc-recruitment
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ZinT (YodA) periplasmic lipocalin-like zinc-recruitment Provide feedback
ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families PF01297 PF00005 regulated by the transcription-regulator FUR, PF01475 [2,3]. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), PF01297 . Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination .
Gabbianelli R, Scotti R, Ammendola S, Petrarca P, Nicolini L, Battistoni A;, BMC Microbiol. 2011;11:36.: Role of ZnuABC and ZinT in Escherichia coli O157:H7 zinc acquisition and interaction with epithelial cells. PUBMED:21338480 EPMC:21338480
Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D, Falconi M, Chiancone E;, Biochim Biophys Acta. 2014;1840:535-544.: The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc. PUBMED:24128931 EPMC:24128931
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This tab holds annotation information from the InterPro database.
InterPro entry IPR015304
This domain is found in prokaryotic proteins that were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium and ensure its subsequent elimination [PUBMED:12909634]. Previously known YodA, these proteins have been renamed as ZinT, and have been shown to bind zinc with high affinity. They may play a role in zinc homeostasis and growth under zinc limited conditions [PUBMED:17931600].
|Molecular function||zinc ion binding (GO:0008270)|
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The calycin structural superfamily [1-3] includes the lipocalins, the fatty acid-binding proteins (FABPs).
The clan contains the following 37 members:ApoM Calycin_like CpeS CpeT CrtC DUF1794 DUF1934 DUF2147 DUF3255 DUF3598 DUF3642 DUF4488 DUF4822 DUF4847 DUF5004 His_binding Lipocalin Lipocalin_2 Lipocalin_3 Lipocalin_4 Lipocalin_5 Lipocalin_7 Lipocalin_8 Lipocalin_9 Luciferase_cat META MoaF MoaF_C MxiM Nitrophorin NlpE PA_decarbox Svf1 Svf1_C Triabin VDE ZinT
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Author:||Sammut SJ, Bateman A|
|Number in seed:||49|
|Number in full:||274|
|Average length of the domain:||174.70 aa|
|Average identity of full alignment:||43 %|
|Average coverage of the sequence by the domain:||51.66 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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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 ZinT domain has been found. There are 9 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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