ID   ERFK_SALTY              Reviewed;         309 AA.
AC   P40680;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable L,D-transpeptidase ErfK/SrfK;
DE            EC=2.-.-.-;
DE   Flags: Precursor;
GN   Name=erfK; Synonyms=srfK; OrderedLocusNames=STM2015;
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 [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=7883701; DOI=10.1128/jb.177.6.1461-1469.1995;
RA   Chen P., Ailion M., Weyand N., Roth J.R.;
RT   "The end of the cob operon: evidence that the last gene (cobT) catalyzes
RT   synthesis of the lower ligand of vitamin B12, dimethylbenzimidazole.";
RL   J. Bacteriol. 177:1461-1469(1995).
RN   [2]
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the YkuD family. {ECO:0000305}.
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DR   EMBL; L35477; AAA69298.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20919.1; -; Genomic_DNA.
DR   RefSeq; NP_460960.1; NC_003197.2.
DR   RefSeq; WP_001252816.1; NC_003197.2.
DR   AlphaFoldDB; P40680; -.
DR   SMR; P40680; -.
DR   STRING; 99287.STM2015; -.
DR   PaxDb; P40680; -.
DR   EnsemblBacteria; AAL20919; AAL20919; STM2015.
DR   GeneID; 1253536; -.
DR   KEGG; stm:STM2015; -.
DR   PATRIC; fig|99287.12.peg.2137; -.
DR   HOGENOM; CLU_046834_0_1_6; -.
DR   OMA; KQEGPTW; -.
DR   PhylomeDB; P40680; -.
DR   BioCyc; SENT99287:STM2015-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0018104; P:peptidoglycan-protein cross-linking; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.40.440.10; -; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR041597; Ldt_C.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   Pfam; PF17969; Ldt_C; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; SSF141523; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Hydrolase; Peptidoglycan synthesis; Periplasm; Reference proteome; Signal;
KW   Transferase.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..309
FT                   /note="Probable L,D-transpeptidase ErfK/SrfK"
FT                   /id="PRO_0000021196"
SQ   SEQUENCE   309 AA;  34180 MW;  55CCBEE5FEBDC259 CRC64;
     MRRITPFFPF FVLLVSHFSL AISYPLPPEG SRLVGQPVTI AVPQNNTQPL ESFAARYGQG
     LSNMLEANPG VDVFLPQSGS TLVVPQQLIL PDTVREGIVV NVAEMRLYYY PAGTNTVEVL
     PIGIGQAGRE TPRNWVTAVE RKQDGPVWVP TANTRREYAK EGKTLPAMVP AGPDNPMGLY
     AIYIGRLYAI HGTNANFGIG LRVSQGCIRL RNDDIKYLFD HVPVGTRVQI IDRPVKFSVE
     PDGSRWLEVH EPLSRNRAEF ESDKKVPLPV TPVLRTFIKG DDVDTSRVNE VLERRSGMPV
     NISAGRPGL