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Database: UniProt
Entry: A0A2Z4UDZ9_9FIRM
LinkDB: A0A2Z4UDZ9_9FIRM
Original site: A0A2Z4UDZ9_9FIRM 
ID   A0A2Z4UDZ9_9FIRM        Unreviewed;       115 AA.
AC   A0A2Z4UDZ9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Hydrogenase maturation factor HypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN   Name=hypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN   ORFNames=DQQ01_15695 {ECO:0000313|EMBL:AWY99325.1};
OS   Blautia argi.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1912897 {ECO:0000313|EMBL:AWY99325.1, ECO:0000313|Proteomes:UP000250003};
RN   [1] {ECO:0000313|Proteomes:UP000250003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 15426 {ECO:0000313|Proteomes:UP000250003};
RA   Chang Y.-H., Paek J., Shin Y.;
RT   "Description of Blautia argi sp. nov., a new anaerobic isolated from dog
RT   feces.";
RL   Submitted (JUN-2018) 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. {ECO:0000256|HAMAP-
CC       Rule:MF_00213}.
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DR   EMBL; CP030280; AWY99325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z4UDZ9; -.
DR   KEGG; blau:DQQ01_15695; -.
DR   OrthoDB; 9800361at2; -.
DR   Proteomes; UP000250003; Chromosome.
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; 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.
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:UP000250003};
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         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
SQ   SEQUENCE   115 AA;  12962 MW;  1B7587698674E330 CRC64;
     MHELGVVFHV IKTVEEVAKE NQLTEIEAVT LQLGEVSGVI ESYLQNCWKW AVEKKSEILK
     ESALVVETIP AVTFCEDCEK TYGTVEHGKI CPYCGSERTY LQQGNEFFIK EISGC
//
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