ID   YBIS_ECOL6              Reviewed;         306 AA.
AC   P0AAX9; P75789;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable L,D-transpeptidase YbiS;
DE            EC=2.-.-.-;
DE   Flags: Precursor;
GN   Name=ybiS; OrderedLocusNames=c0905;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Responsible, at least in part, for anchoring of the major
CC       outer membrane lipoprotein (Lpp) to the peptidoglycan via a meso-
CC       diaminopimelyl-L-Lys- bond on the terminal residue of Lpp.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the YkuD family. {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; AE014075; AAN79378.1; -; Genomic_DNA.
DR   RefSeq; WP_001056384.1; NC_004431.1.
DR   AlphaFoldDB; P0AAX9; -.
DR   SMR; P0AAX9; -.
DR   STRING; 199310.c0905; -.
DR   EnsemblBacteria; AAN79378; AAN79378; c0905.
DR   GeneID; 66670908; -.
DR   KEGG; ecc:c0905; -.
DR   eggNOG; COG1376; Bacteria.
DR   HOGENOM; CLU_046834_0_1_6; -.
DR   OMA; QNRSGMP; -.
DR   BioCyc; ECOL199310:C0905-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001410; 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; IEA:UniProt.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; Signal; Transferase.
FT   SIGNAL          1..24
FT   CHAIN           25..306
FT                   /note="Probable L,D-transpeptidase YbiS"
FT                   /id="PRO_0000042567"
SQ   SEQUENCE   306 AA;  33325 MW;  4D9DDED8B0ACD69F CRC64;
     MNMKLKTLFA AAFAVVGFCS TASAVTYPLP TDGSRLVGQN QVITIPEGNT QPLEYFAAEY
     QMGLSNMMEA NPGVDTFLPK GGTVLNIPQQ LILPDTVHEG IVINSAEMRL YYYPKGTNTV
     IVLPIGIGQL GKDTPINWTT KVERKKAGPT WTPTAKMHAE YRAAGEPLPA VVPAGPDNPM
     GLYALYIGRL YAIHGTNANF GIGLRVSHGC VRLRNEDIKF LFEKVPVGTR VQFIDEPVKA
     TTEPDGSRYI EVHNPLSTTE AQFEGQEIVP ITLTKSVQTV TGQPDVDQVV LDEAIKNRSG
     MPVRLN