ID A2SJN1_METPP Unreviewed; 114 AA.
AC A2SJN1;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Hydrogenase maturation factor HypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN Name=hypA {ECO:0000256|HAMAP-Rule:MF_00213};
GN OrderedLocusNames=Mpe_A2816 {ECO:0000313|EMBL:ABM95770.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM95770.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM95770.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(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.
CC {ECO:0000256|ARBA:ARBA00010748, ECO:0000256|HAMAP-Rule:MF_00213}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000555; ABM95770.1; -; Genomic_DNA.
DR RefSeq; WP_011830399.1; NC_008825.1.
DR AlphaFoldDB; A2SJN1; -.
DR STRING; 420662.Mpe_A2816; -.
DR KEGG; mpt:Mpe_A2816; -.
DR eggNOG; COG0375; Bacteria.
DR HOGENOM; CLU_126929_0_0_4; -.
DR Proteomes; UP000000366; 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; 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:UP000000366};
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; 12272 MW; 35F19C47D872D44D CRC64;
MHEASLAGGI LKLVEDAAQR EGFRSVTVLR MEAGRLAGVE VRALQFALES LAPGTCLQDA
RFEIEEPIGQ AWCLHCSQTV EIAQRGDACP VCGGYQVQPT GGTELRVLDM LVDD
//
