YHJJ_SALTY
ID YHJJ_SALTY Reviewed; 495 AA.
AC P50335;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein YhjJ;
DE Flags: Precursor;
GN Name=yhjJ; OrderedLocusNames=STM3613;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-287.
RC STRAIN=LT2;
RX PubMed=8955389; DOI=10.1128/jb.178.24.7099-7105.1996;
RA Baker K.E., Ditullio K.P., Neuhard J., Kelln R.A.;
RT "Utilization of orotate as a pyrimidine source by Salmonella typhimurium
RT and Escherichia coli requires the dicarboxylate transport protein encoded
RT by dctA.";
RL J. Bacteriol. 178:7099-7105(1996).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Has lost the active site residues.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA62743.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL22473.1; -; Genomic_DNA.
DR EMBL; X91397; CAA62743.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_462514.1; NC_003197.2.
DR RefSeq; WP_001163182.1; NC_003197.2.
DR AlphaFoldDB; P50335; -.
DR SMR; P50335; -.
DR STRING; 99287.STM3613; -.
DR PaxDb; P50335; -.
DR EnsemblBacteria; AAL22473; AAL22473; STM3613.
DR GeneID; 1255136; -.
DR KEGG; stm:STM3613; -.
DR PATRIC; fig|99287.12.peg.3819; -.
DR HOGENOM; CLU_043932_0_0_6; -.
DR OMA; FWHVQQN; -.
DR PhylomeDB; P50335; -.
DR BioCyc; SENT99287:STM3613-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
PE 3: Inferred from homology;
KW Hydrolase; Metalloprotease; Periplasm; Protease; Reference proteome;
KW Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..495
FT /note="Protein YhjJ"
FT /id="PRO_0000026766"
FT CONFLICT 244
FT /note="G -> L (in Ref. 2; CAA62743)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..287
FT /note="DTPWQPIR -> IRRGNRFA (in Ref. 2; CAA62743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 55181 MW; 59D6A0198E0B23B7 CRC64;
MQGTKIRLLA GSLLMLASAG YVQADALQPD PAWQQGTLAN GLQWQVLATP QRPSDRIEVR
LQVNTGSLTE STQQSGFSHA IPRIALTQSG GLDAAQARSL WQQGFDPKRP MPPVIVSYDS
TLYNLSLPNN RNDLLKEALT YLANVSGKLT ITPETVNHAL SSEDMVATWP ADTKEGWWRY
RLKGSALLGH DPAEPLKQPV DAAKIQAFYE KWYTPDAMTL IVVGNIDARS VAEQINKTFG
TLKGKRETPA PVPTLSPLRA ESVSIMTDAV RQDRLSIMWD TPWQPIRESA ALLRYWQADL
AREALFWHIQ QELTKNNAKD IGLGFDCRVL FLRAQCAINI ESPNDKLNTN LSLVANELAK
VRDKGLSEEE FTALVAQKNL ELQKLFATYA RTDTDILTGQ RMRSLQNQVV DIAPEQYQKL
RQNFLNSLTV DMLNQNLRQQ LSQEMALILL QPQGEPEFNM KALKATWDEI MVPTTAAAVE
ADEAHPEVTE TPAAQ