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Database: UniProt
Entry: A0A011MH34_9PROT
LinkDB: A0A011MH34_9PROT
Original site: A0A011MH34_9PROT 
ID   A0A011MH34_9PROT        Unreviewed;       113 AA.
AC   A0A011MH34;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
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:EXI69213.1};
GN   ORFNames=AW08_00420 {ECO:0000313|EMBL:EXI69213.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI69213.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI69213.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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.
CC       {ECO:0000256|ARBA:ARBA00010748, ECO:0000256|HAMAP-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:EXI69213.1}.
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DR   EMBL; JFAX01000002; EXI69213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011MH34; -.
DR   STRING; 1454001.AW08_00420; -.
DR   PATRIC; fig|1454001.3.peg.383; -.
DR   Proteomes; UP000020218; 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; IPR020538; Hydgase_Ni_incorp_HypA/HybF_CS.
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.
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:UP000020218};
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;  11908 MW;  70E4F39BFE2CD1C5 CRC64;
     MHEMSLAVGI VDLIEEAARA QGFRRVLTVA IEIGELAAVE AEAIGFCFSA VTRGTLAEGA
     RLQIVQVPGE GLCFNCHQTV PLAALYDPCP ACGGHPVQAT GGTEMRVKEL EVE
//
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