HYCI_ECOLI
ID HYCI_ECOLI Reviewed; 156 AA.
AC P0AEV9; Q2MAB2; Q57451;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Hydrogenase 3 maturation protease;
DE EC=3.4.23.51 {ECO:0000269|PubMed:10727938};
DE AltName: Full=HycI protease;
GN Name=hycI; OrderedLocusNames=b2717, JW2687;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-37 AND 66-84.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=7851435; DOI=10.1111/j.1432-1033.1995.tb20422.x;
RA Rossmann R., Maier T., Lottspeich F., Boeck A.;
RT "Characterisation of a protease from Escherichia coli involved in
RT hydrogenase maturation.";
RL Eur. J. Biochem. 227:545-550(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP MUTAGENESIS OF ASP-16; ASP-62 AND HIS-90, INVOLVEMENT OF NICKEL ION BINDING
RP IN PROTEASE ACTIVITY, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=10727938; DOI=10.1046/j.1432-1327.2000.01202.x;
RA Theodoratou E., Paschos A., Magalon A., Fritsche E., Huber R., Boeck A.;
RT "Nickel serves as a substrate recognition motif for the endopeptidase
RT involved in hydrogenase maturation.";
RL Eur. J. Biochem. 267:1995-1999(2000).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=17150961; DOI=10.1074/jbc.m609263200;
RA Yang F., Hu W., Xu H., Li C., Xia B., Jin C.;
RT "Solution structure and backbone dynamics of an endopeptidase HycI from
RT Escherichia coli: implications for mechanism of the [NiFe] hydrogenase
RT maturation.";
RL J. Biol. Chem. 282:3856-3863(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-156 IN COMPLEX WITH CALCIUM
RP IONS.
RX PubMed=19720045; DOI=10.1016/j.bbrc.2009.08.135;
RA Kumarevel T., Tanaka T., Bessho Y., Shinkai A., Yokoyama S.;
RT "Crystal structure of hydrogenase maturating endopeptidase HycI from
RT Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 389:310-314(2009).
CC -!- FUNCTION: Protease involved in the C-terminal processing of HycE, the
CC large subunit of hydrogenase 3. {ECO:0000269|PubMed:10727938}.
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:0000269|PubMed:10727938};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19720045}.
CC -!- INTERACTION:
CC P0AEV9; P0AFG8: aceE; NbExp=2; IntAct=EBI-552628, EBI-542683;
CC -!- SIMILARITY: Belongs to the peptidase A31 family. {ECO:0000305}.
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DR EMBL; X17506; CAA35554.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69227.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75759.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76794.1; -; Genomic_DNA.
DR PIR; S67469; S67469.
DR RefSeq; NP_417197.1; NC_000913.3.
DR RefSeq; WP_000132961.1; NZ_SSZK01000017.1.
DR PDB; 2E85; X-ray; 1.70 A; A/B=1-156.
DR PDB; 2I8L; NMR; -; A=1-156.
DR PDBsum; 2E85; -.
DR PDBsum; 2I8L; -.
DR AlphaFoldDB; P0AEV9; -.
DR SMR; P0AEV9; -.
DR BioGRID; 4261309; 13.
DR DIP; DIP-48019N; -.
DR IntAct; P0AEV9; 9.
DR STRING; 511145.b2717; -.
DR MEROPS; A31.003; -.
DR jPOST; P0AEV9; -.
DR PaxDb; P0AEV9; -.
DR PRIDE; P0AEV9; -.
DR EnsemblBacteria; AAC75759; AAC75759; b2717.
DR EnsemblBacteria; BAE76794; BAE76794; BAE76794.
DR GeneID; 67413985; -.
DR GeneID; 947428; -.
DR KEGG; ecj:JW2687; -.
DR KEGG; eco:b2717; -.
DR PATRIC; fig|1411691.4.peg.4024; -.
DR EchoBASE; EB3177; -.
DR eggNOG; COG0680; Bacteria.
DR HOGENOM; CLU_099037_4_0_6; -.
DR InParanoid; P0AEV9; -.
DR OMA; EMCAANP; -.
DR PhylomeDB; P0AEV9; -.
DR BioCyc; EcoCyc:G7414-MON; -.
DR BioCyc; MetaCyc:G7414-MON; -.
DR BRENDA; 3.4.23.51; 2026.
DR EvolutionaryTrace; P0AEV9; -.
DR PRO; PR:P0AEV9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase activity; IDA:EcoCyc.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Direct protein sequencing; Hydrolase;
KW Metal-binding; Nickel; Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7851435"
FT CHAIN 2..156
FT /note="Hydrogenase 3 maturation protease"
FT /id="PRO_0000201944"
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"
FT MUTAGEN 16
FT /note="D->N: No protease activity."
FT /evidence="ECO:0000269|PubMed:10727938"
FT MUTAGEN 62
FT /note="D->N,M: No protease activity."
FT /evidence="ECO:0000269|PubMed:10727938"
FT MUTAGEN 90
FT /note="H->Q: A little protease activity remaining."
FT /evidence="ECO:0000269|PubMed:10727938"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2E85"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:2E85"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:2E85"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2E85"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2E85"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:2E85"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:2E85"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2E85"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2E85"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2I8L"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2I8L"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:2E85"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:2E85"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:2E85"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2I8L"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:2E85"
SQ SEQUENCE 156 AA; 17057 MW; CCE90535AFC0F30D CRC64;
MTDVLLCVGN SMMGDDGAGP LLAEKCAAAP KGNWVVIDGG SAPENDIVAI RELRPTRLLI
VDATDMGLNP GEIRIIDPDD IAEMFMMTTH NMPLNYLIDQ LKEDIGEVIF LGIQPDIVGF
YYPMTQPIKD AVETVYQRLE GWEGNGGFAQ LAVEEE
