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Database: UniProt
Entry: A0A0Q4XRE0_9BURK
LinkDB: A0A0Q4XRE0_9BURK
Original site: A0A0Q4XRE0_9BURK 
ID   A0A0Q4XRE0_9BURK        Unreviewed;       114 AA.
AC   A0A0Q4XRE0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Hydrogenase maturation factor HypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN   Name=hypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN   ORFNames=ASF43_13270 {ECO:0000313|EMBL:KQP15011.1};
OS   Pseudorhodoferax sp. Leaf267.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP15011.1, ECO:0000313|Proteomes:UP000051560};
RN   [1] {ECO:0000313|EMBL:KQP15011.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP15011.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP15011.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP15011.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required
CC       for nickel insertion into the metal center of the hydrogenase.
CC       {ECO:0000256|HAMAP-Rule:MF_00213}.
CC   -!- SIMILARITY: Belongs to the HypA/HybF family.
CC       {ECO:0000256|ARBA:ARBA00010748, ECO:0000256|HAMAP-Rule:MF_00213}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQP15011.1}.
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DR   EMBL; LMMV01000021; KQP15011.1; -; Genomic_DNA.
DR   RefSeq; WP_056184198.1; NZ_LMMV01000021.1.
DR   AlphaFoldDB; A0A0Q4XRE0; -.
DR   STRING; 1736316.ASF43_13270; -.
DR   OrthoDB; 288014at2; -.
DR   Proteomes; UP000051560; Unassembled WGS sequence.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051604; P:protein maturation; IEA:InterPro.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.2320.80; -; 1.
DR   HAMAP; MF_00213; HypA_HybF; 1.
DR   InterPro; IPR020538; Hydgase_Ni_incorp_HypA/HybF_CS.
DR   InterPro; IPR000688; HypA/HybF.
DR   PANTHER; PTHR34535; HYDROGENASE MATURATION FACTOR HYPA; 1.
DR   PANTHER; PTHR34535:SF3; HYDROGENASE MATURATION FACTOR HYPA; 1.
DR   Pfam; PF01155; HypA; 1.
DR   PIRSF; PIRSF004761; Hydrgn_mat_HypA; 1.
DR   PROSITE; PS01249; HYPA; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00213};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_00213};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051560};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00213}.
FT   BINDING         2
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
SQ   SEQUENCE   114 AA;  12184 MW;  458263CD0B7B50CB CRC64;
     MHEASLAGGV LQLVDDTAAR EGFARVTLLR LEVGALAGVE LRALQFALEA IAPGTRLADA
     RFEFDEPPGQ AWCMGCARST PLARRGDACT HCGDYRVQPT GGAELRVVEM LVED
//
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