ID   HUPD_THIRO              Reviewed;         221 AA.
AC   Q56362;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Hydrogenase expression/formation protein HupD;
GN   Name=hupD;
OS   Thiocapsa roseopersicina.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocapsa.
OX   NCBI_TaxID=1058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8125335; DOI=10.1016/0378-1119(94)90726-9;
RA   Colbeau A.A., Kovacs K.K., Chabert J.J., Vignais P.P.M.;
RT   "Cloning and sequence of the structural (hupSLC) and accessory (hupDHI)
RT   genes for hydrogenase biosynthesis in Thiocapsa roseopersicina.";
RL   Gene 140:25-31(1994).
CC   -!- FUNCTION: Not known. Could be involved in the processing of
CC       hydrogenase.
CC   -!- SIMILARITY: Belongs to the peptidase A31 family. {ECO:0000305}.
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DR   EMBL; L22980; AAA27412.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q56362; -.
DR   SMR; Q56362; -.
DR   MEROPS; A31.002; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016485; P:protein processing; IEA:InterPro.
DR   Gene3D; 3.40.50.1450; -; 1.
DR   InterPro; IPR004419; Pept_A31_hyd_express.
DR   InterPro; IPR023430; Pept_HybD-like_dom_sf.
DR   InterPro; IPR000671; Peptidase_A31.
DR   PANTHER; PTHR30302; PTHR30302; 1.
DR   Pfam; PF01750; HycI; 1.
DR   PRINTS; PR00446; HYDRGNUPTAKE.
DR   SUPFAM; SSF53163; SSF53163; 1.
DR   TIGRFAMs; TIGR00140; hupD; 1.
DR   TIGRFAMs; TIGR00072; hydrog_prot; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Hydrolase; Metal-binding; Nickel; Protease.
FT   CHAIN           1..221
FT                   /note="Hydrogenase expression/formation protein HupD"
FT                   /id="PRO_0000201941"
FT   BINDING         20
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   221 AA;  24341 MW;  ED9ECB3F169E2C1D CRC64;
     MRSDPEILVL GIGNLLWADE GFGVRAVEAL QRHWVMSSNV QLLDGGTQGI YLVDRVRKAD
     VLVVFDAVDY GLPPGTMKRV EDDEVPRFLG AKKMSLHQTG FQEVLALAAM LGDYPKHLLL
     IGVQPVELDD FGGSLRPQIK ERITPAIEMA LEYLAQFGVV ARRREDSTVD SPHLPHPSLD
     LIAYESGRPG PEIACRIGDE RVLTSLSART VQPGNPHGDR Q