SGCX_ECOLI
ID SGCX_ECOLI Reviewed; 373 AA.
AC P39366; Q2M609;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Putative aminopeptidase SgcX;
DE EC=3.4.11.-;
GN Name=sgcX; Synonyms=yjhO; OrderedLocusNames=b4305, JW5776;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 125.
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 DISCUSSION OF SEQUENCE.
RA Reizer J., Charbit A., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferases system genes revealed by bacterial genome
RT analysis: operons encoding homologues of sugar-specific permease domains of
RT the phosphotransferase system and pentose catabolic enzymes.";
RL Genome Sci. Technol. 1:53-75(1996).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97201.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U14003; AAA97201.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77261.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78297.1; -; Genomic_DNA.
DR PIR; C65244; C65244.
DR RefSeq; NP_418725.4; NC_000913.3.
DR RefSeq; WP_000010829.1; NZ_SSUV01000012.1.
DR AlphaFoldDB; P39366; -.
DR SMR; P39366; -.
DR BioGRID; 4262743; 3.
DR DIP; DIP-10881N; -.
DR STRING; 511145.b4305; -.
DR MEROPS; M42.A01; -.
DR PaxDb; P39366; -.
DR PRIDE; P39366; -.
DR EnsemblBacteria; AAC77261; AAC77261; b4305.
DR EnsemblBacteria; BAE78297; BAE78297; BAE78297.
DR GeneID; 948840; -.
DR KEGG; ecj:JW5776; -.
DR KEGG; eco:b4305; -.
DR PATRIC; fig|1411691.4.peg.2391; -.
DR EchoBASE; EB2445; -.
DR eggNOG; COG1363; Bacteria.
DR HOGENOM; CLU_047249_0_1_6; -.
DR InParanoid; P39366; -.
DR OMA; FGWPAIH; -.
DR PhylomeDB; P39366; -.
DR BioCyc; EcoCyc:SGCB-MON; -.
DR PRO; PR:P39366; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.40; -; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome.
FT CHAIN 1..373
FT /note="Putative aminopeptidase SgcX"
FT /id="PRO_0000071656"
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 125
FT /note="G -> A (in Ref. 1; AAA97201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 40615 MW; CAC872934C3A017A CRC64;
MSFSVQETLF SLLQHNAISG HENAVADVML CEFRRQAKEV WRDRLGNVVA RYGSDKPDAL
RLMIFAHMDE VGFMVRKIEP SGFLRFERVG GPAQVTMAGS IVTLTGDKGP VMGCIGIKSY
HFAKGDERTQ SPSVDKLWID IGAKDKDDAI RMGIQVGTPV TLYNPPQLLA NDLVCSKALD
DRLGCTALLG VADAISTMEL DIAVYLVASV QEEFNIRGIV PVLRRVKPDL AIGIDITPSC
DTPDLHDYSE VRINQGVGIT CLNYHGRGTL AGLITPPRLI RMLEQTALEH NIPVQREVAP
GVITETGYIQ VEQDGIPCAS LSIPCRYTHS PAEVASLRDL TDCIRLLTAL AGMSAAHFPV
EPDSGTTQEA HPL
