ID   HOXM_CUPNH              Reviewed;         202 AA.
AC   P31909;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Hydrogenase expression/formation protein HoxM;
GN   Name=hoxM; OrderedLocusNames=PHG005;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1383192; DOI=10.1128/jb.174.19.6277-6289.1992;
RA   Kortlueke C., Horstmann K., Schwartz E., Rohde M., Binsack R.,
RA   Friedrich B.;
RT   "A gene complex coding for the membrane-bound hydrogenase of Alcaligenes
RT   eutrophus H16.";
RL   J. Bacteriol. 174:6277-6289(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT   encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(2003).
CC   -!- FUNCTION: Absolutely required for hydrogenase activity. Mediates the
CC       attachment of hydrogenase to the bacterial membrane; attachment is a
CC       requirement for enzymatic activity.
CC   -!- SIMILARITY: Belongs to the peptidase A31 family. {ECO:0000305}.
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DR   EMBL; M96433; AAA16465.1; -; Unassigned_DNA.
DR   EMBL; AY305378; AAP85761.1; -; Genomic_DNA.
DR   PIR; E43255; E43255.
DR   AlphaFoldDB; P31909; -.
DR   SMR; P31909; -.
DR   STRING; 381666.PHG005; -.
DR   MEROPS; A31.002; -.
DR   EnsemblBacteria; AAP85761; AAP85761; PHG005.
DR   KEGG; reh:PHG005; -.
DR   eggNOG; COG0680; Bacteria.
DR   HOGENOM; CLU_099037_0_1_4; -.
DR   OMA; MGAKKMS; -.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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; Plasmid; Protease;
KW   Reference proteome.
FT   CHAIN           1..202
FT                   /note="Hydrogenase expression/formation protein HoxM"
FT                   /id="PRO_0000201935"
FT   BINDING         15
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   202 AA;  22254 MW;  FAABB5BC869EC150 CRC64;
     MVVAMGIGNV LWADEGFGVR CIETLQQRYQ FAPQVCLVDG GTQGLYLIHH VQAASRLLIF
     DAIDYGLPPG TLRIIEDEAV PKFLGAKKMS LHQTGFQEVL LLAQLTGQYP QQVVLIGCQP
     EELEDYGGSL RRVMKAAVED AVEKGADLLR RWGGMPVPRT AELAPAEAVT VPHLALDRYE
     AERPSPRAAC RIGDERFMPQ DL