ID   SGCX_SALTY              Reviewed;         372 AA.
AC   P58535;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Putative aminopeptidase SgcX;
DE            EC=3.4.11.-;
GN   Name=sgcX; OrderedLocusNames=STM1612;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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}.
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DR   EMBL; AE006468; AAL20530.1; -; Genomic_DNA.
DR   RefSeq; NP_460571.1; NC_003197.2.
DR   RefSeq; WP_000144617.1; NC_003197.2.
DR   AlphaFoldDB; P58535; -.
DR   SMR; P58535; -.
DR   STRING; 99287.STM1612; -.
DR   MEROPS; M42.A01; -.
DR   PaxDb; P58535; -.
DR   EnsemblBacteria; AAL20530; AAL20530; STM1612.
DR   GeneID; 1253130; -.
DR   KEGG; stm:STM1612; -.
DR   PATRIC; fig|99287.12.peg.1703; -.
DR   HOGENOM; CLU_047249_0_1_6; -.
DR   OMA; FGWPAIH; -.
DR   PhylomeDB; P58535; -.
DR   BioCyc; SENT99287:STM1612-MON; -.
DR   Proteomes; UP000001014; 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..372
FT                   /note="Putative aminopeptidase SgcX"
FT                   /id="PRO_0000071658"
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"
SQ   SEQUENCE   372 AA;  40459 MW;  9A5A1A3D99D509E1 CRC64;
     MTFSVQETLF SLLRLNGISG HENSIANVMQ HAFEQQAKDV WRDRLGNVVA RYGSDKPDAL
     RLMIFAHMDE VGFMVRKIEP SGFLRFERVG GPAQITMPGS IVTLAGRSGD IMGCIGIKAY
     HFAKGDERTQ PPALDKLWID IGAKDKADAE RMGIQVGTPV TLYNPPHCLG NDLVCSKALD
     DRLGCTALLG VAEALASTPL DIAVFLVASV QEEFNIRGII PVLRRVRPDL AIGIDITPSC
     DTPDLQDYSD VRVNHGVGIT CLNYHGRGTL AGLITPPRLL RMLETTAHEN NIPVQREVAP
     GVITETGYIQ VELDGIPCAS LSIPCRYTHS PAEVASLRDL ADCIRLLTAL ANMSPEQFPI
     EPETGATQEA RP