ID   A0A1M7XZS7_9FIRM        Unreviewed;       118 AA.
AC   A0A1M7XZS7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Hydrogenase maturation factor HypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN   Name=hypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN   ORFNames=SAMN02745217_00687 {ECO:0000313|EMBL:SHO44687.1};
OS   Anaerocolumna xylanovorans DSM 12503.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerocolumna.
OX   NCBI_TaxID=1121345 {ECO:0000313|EMBL:SHO44687.1, ECO:0000313|Proteomes:UP000184612};
RN   [1] {ECO:0000313|EMBL:SHO44687.1, ECO:0000313|Proteomes:UP000184612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12503 {ECO:0000313|EMBL:SHO44687.1,
RC   ECO:0000313|Proteomes:UP000184612};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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; FRFD01000003; SHO44687.1; -; Genomic_DNA.
DR   RefSeq; WP_073587368.1; NZ_FRFD01000003.1.
DR   AlphaFoldDB; A0A1M7XZS7; -.
DR   STRING; 1121345.SAMN02745217_00687; -.
DR   OrthoDB; 9800361at2; -.
DR   Proteomes; UP000184612; 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; 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:UP000184612};
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         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
SQ   SEQUENCE   118 AA;  13294 MW;  8F9CAD5FBC19BA15 CRC64;
     MHEITILVQL VNMVEKEAKA NHIAEKIDTI VVQLGQLTSI VPKYLTEYYP NVTEGTKLSG
     SKLEIERIPG NGLCHHCNKV LRIVEHKGKC PICGADDWEM LSGQEFILKE IRVREAVV
//