HUPD_RHILV
ID HUPD_RHILV Reviewed; 202 AA.
AC P27649; Q52829;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Hydrogenase expression/formation protein HupD;
GN Name=hupD;
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UPM791;
RX PubMed=1597428; DOI=10.1128/jb.174.12.4130-4139.1992;
RA Hidalgo E., Palacios J.M., Murillo J., Ruiz-Argueso T.;
RT "Nucleotide sequence and characterization of four additional genes of the
RT hydrogenase structural operon from Rhizobium leguminosarum bv. viciae.";
RL J. Bacteriol. 174:4130-4139(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B10;
RA Brito B., Palacios J.M., Imperial J., Ruiz-Argueso T., Yang W.C.,
RA Bisseling T., Schmitt H., Kerl V., Bauer T., Kokotek W., Lotz W.;
RT "Organization of the hup-region and its differential transcription in non-
RT symbiotic and symbiotic cells of Rhizobium leguminosarum bv. viciae B10.";
RL Mol. Plant Microbe Interact. 8:235-240(1997).
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; X52974; CAA37151.1; -; Genomic_DNA.
DR EMBL; Z36981; CAA85433.1; -; Genomic_DNA.
DR PIR; B41892; B41892.
DR RefSeq; WP_018517048.1; NZ_WIDT01000003.1.
DR AlphaFoldDB; P27649; -.
DR SMR; P27649; -.
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..202
FT /note="Hydrogenase expression/formation protein HupD"
FT /id="PRO_0000201939"
FT BINDING 28
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT CONFLICT 72
FT /note="V -> G (in Ref. 1; CAA37151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22089 MW; BD7E5A2053D38942 CRC64;
MTIPYPLGPP PAPRILVLGI GNILWADEGF GVRAVEAFHK AYELSDNVTI LDGGTQGLYL
VQFVNEHDRL IVFDAIDYGL EPGTMKVVED DEVPKFTGAK KMSLHQTGFQ EVLSAADFMG
HYPERLTLIG CQPLDLEDWG GPLTAPVRGV IPAAIETAVR VLRSWGVAVT ARPEGAAVPP
LLEHDIDFER YERRAEPAAL NC