YCFS_ECOLI
ID YCFS_ECOLI Reviewed; 320 AA.
AC P75954;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable L,D-transpeptidase YcfS;
DE EC=2.-.-.-;
DE Flags: Precursor;
GN Name=ycfS; OrderedLocusNames=b1113, JW5820;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=18456808; DOI=10.1128/jb.00025-08;
RA Magnet S., Dubost L., Marie A., Arthur M., Gutmann L.;
RT "Identification of the L,D-transpeptidases for peptidoglycan cross-linking
RT in Escherichia coli.";
RL J. Bacteriol. 190:4782-4785(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DSBG.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=19965429; DOI=10.1126/science.1179557;
RA Depuydt M., Leonard S.E., Vertommen D., Denoncin K., Morsomme P., Wahni K.,
RA Messens J., Carroll K.S., Collet J.F.;
RT "A periplasmic reducing system protects single cysteine residues from
RT oxidation.";
RL Science 326:1109-1111(2009).
CC -!- FUNCTION: Responsible, at least in part, for anchoring of the major
CC outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein)
CC to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the
CC terminal residue of Lpp. {ECO:0000269|PubMed:18456808}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBUNIT: Interacts with DsbG. {ECO:0000269|PubMed:19965429}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous disruption of erfK, ybiS, ycfS and
CC ynhG leads to loss of covalent anchoring of the major outer membrane
CC lipoprotein (Lpp) to the peptidoglycan. Complementation with ycfS
CC restores some of this anchoring. {ECO:0000269|PubMed:18456808}.
CC -!- SIMILARITY: Belongs to the YkuD family. {ECO:0000305}.
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DR EMBL; U00096; AAC74197.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35928.1; -; Genomic_DNA.
DR PIR; F64855; F64855.
DR RefSeq; NP_415631.1; NC_000913.3.
DR RefSeq; WP_001350500.1; NZ_CP064683.1.
DR AlphaFoldDB; P75954; -.
DR SMR; P75954; -.
DR BioGRID; 4260085; 12.
DR DIP; DIP-11546N; -.
DR IntAct; P75954; 2.
DR STRING; 511145.b1113; -.
DR MEROPS; C82.A05; -.
DR PaxDb; P75954; -.
DR PRIDE; P75954; -.
DR EnsemblBacteria; AAC74197; AAC74197; b1113.
DR EnsemblBacteria; BAA35928; BAA35928; BAA35928.
DR GeneID; 945666; -.
DR KEGG; ecj:JW5820; -.
DR KEGG; eco:b1113; -.
DR PATRIC; fig|511145.12.peg.1157; -.
DR EchoBASE; EB3211; -.
DR eggNOG; COG1376; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_046834_0_0_6; -.
DR InParanoid; P75954; -.
DR PhylomeDB; P75954; -.
DR BioCyc; EcoCyc:G6571-MON; -.
DR BioCyc; MetaCyc:G6571-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P75954; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0018104; P:peptidoglycan-protein cross-linking; IMP:EcoCyc.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 2.40.440.10; -; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR041597; Ldt_C.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR Pfam; PF17969; Ldt_C; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF03734; YkuD; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF141523; SSF141523; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Hydrolase; Peptidoglycan synthesis; Periplasm; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..320
FT /note="Probable L,D-transpeptidase YcfS"
FT /id="PRO_0000013826"
FT DOMAIN 45..90
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT ACT_SITE 217
FT /evidence="ECO:0000255"
SQ SEQUENCE 320 AA; 34636 MW; 89378A8DFD60359B CRC64;
MMIKTRFSRW LTFFTFAAAV ALALPAKANT WPLPPAGSRL VGENKFHVVE NDGGSLEAIA
KKYNVGFLAL LQANPGVDPY VPRAGSVLTI PLQTLLPDAP REGIVINIAE LRLYYYPPGK
NSVTVYPIGI GQLGGDTLTP TMVTTVSDKR ANPTWTPTAN IRARYKAQGI ELPAVVPAGL
DNPMGHHAIR LAAYGGVYLL HGTNADFGIG MRVSSGCIRL RDDDIKTLFS QVTPGTKVNI
INTPIKVSAE PNGARLVEVH QPLSEKIDDD PQLLPITLNS AMQSFKDAAQ TDAEVMQHVM
DVRSGMPVDV RRHQVSPQTL
