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Database: UniProt
Entry: B1IGX1_CLOBK
LinkDB: B1IGX1_CLOBK
Original site: B1IGX1_CLOBK 
ID   B1IGX1_CLOBK            Unreviewed;       113 AA.
AC   B1IGX1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Hydrogenase maturation factor HypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN   Name=hypA {ECO:0000256|HAMAP-Rule:MF_00213,
GN   ECO:0000313|EMBL:ACA46866.1};
GN   OrderedLocusNames=CLD_2356 {ECO:0000313|EMBL:ACA46866.1};
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA46866.1, ECO:0000313|Proteomes:UP000008541};
RN   [1] {ECO:0000313|EMBL:ACA46866.1, ECO:0000313|Proteomes:UP000008541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000939; ACA46866.1; -; Genomic_DNA.
DR   RefSeq; WP_004451589.1; NC_010516.1.
DR   AlphaFoldDB; B1IGX1; -.
DR   KEGG; cbb:CLD_2356; -.
DR   HOGENOM; CLU_126929_6_0_9; -.
DR   Proteomes; UP000008541; 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   NCBIfam; TIGR00100; hypA; 1.
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   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   113 AA;  12890 MW;  F9991F67A7C5FB29 CRC64;
     MHETAVICEV VDIVLNTAKD NFLEKITKVI LHIGEFSCIQ EDQLKFSYKI ISKDTLLEGS
     DLIIEWVKPL AYCSHCNETF PVSFTHKECP ICHKVSEKIV SGYDTYVYSI EGD
//
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