ID   HYCI_ECO57              Reviewed;         156 AA.
AC   P0AEW0; Q57451;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Hydrogenase 3 maturation protease;
DE            EC=3.4.23.51 {ECO:0000250|UniProtKB:P0AEV9};
DE   AltName: Full=HycI protease;
GN   Name=hycI; OrderedLocusNames=Z4025, ECs3573;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Protease involved in the C-terminal processing of HycE, the
CC       large subunit of hydrogenase 3. {ECO:0000250|UniProtKB:P0AEV9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=This enzyme specifically removes a 32-amino acid peptide from
CC         the C-terminus of the precursor of the large subunit of E.coli
CC         hydrogenase 3 by cleavage at the C-terminal side of Arg-537.;
CC         EC=3.4.23.51; Evidence={ECO:0000250|UniProtKB:P0AEV9};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0AEV9}.
CC   -!- SIMILARITY: Belongs to the peptidase A31 family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG57824.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36996.1; -; Genomic_DNA.
DR   PIR; D85920; D85920.
DR   PIR; E91075; E91075.
DR   RefSeq; NP_311600.1; NC_002695.1.
DR   RefSeq; WP_000132961.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AEW0; -.
DR   SMR; P0AEW0; -.
DR   STRING; 155864.EDL933_3886; -.
DR   MEROPS; A31.003; -.
DR   EnsemblBacteria; AAG57824; AAG57824; Z4025.
DR   EnsemblBacteria; BAB36996; BAB36996; ECs_3573.
DR   GeneID; 67413985; -.
DR   GeneID; 914705; -.
DR   KEGG; ece:Z4025; -.
DR   KEGG; ecs:ECs_3573; -.
DR   PATRIC; fig|386585.9.peg.3734; -.
DR   eggNOG; COG0680; Bacteria.
DR   HOGENOM; CLU_099037_4_0_6; -.
DR   OMA; EMCAANP; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06067; H2MP_MemB-H2evol; 1.
DR   Gene3D; 3.40.50.1450; -; 1.
DR   InterPro; IPR004420; Pept_A31_hyd_mat_HycI.
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; TIGR00142; hycI; 1.
DR   TIGRFAMs; TIGR00072; hydrog_prot; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Hydrolase; Metal-binding; Nickel; Protease;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..156
FT                   /note="Hydrogenase 3 maturation protease"
FT                   /id="PRO_0000201945"
FT   BINDING         16
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   156 AA;  17057 MW;  CCE90535AFC0F30D CRC64;
     MTDVLLCVGN SMMGDDGAGP LLAEKCAAAP KGNWVVIDGG SAPENDIVAI RELRPTRLLI
     VDATDMGLNP GEIRIIDPDD IAEMFMMTTH NMPLNYLIDQ LKEDIGEVIF LGIQPDIVGF
     YYPMTQPIKD AVETVYQRLE GWEGNGGFAQ LAVEEE