ID A0A428J5V4_9BACI Unreviewed; 117 AA.
AC A0A428J5V4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 10.
DE RecName: Full=Hydrogenase maturation factor HypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN Name=hypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN ORFNames=EJF36_10590 {ECO:0000313|EMBL:RSK27293.1};
OS Bacillus sp. HMF5848.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2495421 {ECO:0000313|EMBL:RSK27293.1, ECO:0000313|Proteomes:UP000274811};
RN [1] {ECO:0000313|EMBL:RSK27293.1, ECO:0000313|Proteomes:UP000274811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF5848 {ECO:0000313|EMBL:RSK27293.1,
RC ECO:0000313|Proteomes:UP000274811};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Bacillus sp. HMF5848 Genome sequencing and assembly.";
RL Submitted (DEC-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}.
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:RSK27293.1}.
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DR EMBL; RWIV01000001; RSK27293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428J5V4; -.
DR OrthoDB; 9800361at2; -.
DR Proteomes; UP000274811; 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:UP000274811};
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 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
FT BINDING 79
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"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00213"
SQ SEQUENCE 117 AA; 12911 MW; F32CAC7675E74B60 CRC64;
MHEIALMGDI LNLIEEDSEN RGVKEIQTVE LIVGDLSNAL PDALQMAFDI FKAQKITRLT
ESAELIICRE KALAACTICG LEYVPTHKLT ECPTCKIPSG RLLQGETFQV RAYEGSS
//