YNHG_ECOLI
ID YNHG_ECOLI Reviewed; 334 AA.
AC P76193; P76899; P76900;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable L,D-transpeptidase YnhG;
DE EC=2.-.-.-;
DE Flags: Precursor;
GN Name=ynhG; OrderedLocusNames=b1678, JW1668;
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 / 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-233.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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 generating a meso-
CC diaminopimelyl-3-a meso-diaminopimelyl-3 cross-link.
CC {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. Overexpression of ynhG in this
CC background increases meso-diaminopimelyl-3-a meso-diaminopimelyl-3
CC cross-links but does not restore Lpp anchoring.
CC {ECO:0000269|PubMed:18456808}.
CC -!- SIMILARITY: Belongs to the YkuD family. {ECO:0000305}.
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DR EMBL; U00096; AAC74748.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15458.2; -; Genomic_DNA.
DR PIR; F64925; F64925.
DR RefSeq; NP_416193.1; NC_000913.3.
DR RefSeq; WP_000817105.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P76193; -.
DR SMR; P76193; -.
DR BioGRID; 4260277; 19.
DR DIP; DIP-12774N; -.
DR IntAct; P76193; 1.
DR STRING; 511145.b1678; -.
DR MEROPS; C82.A03; -.
DR jPOST; P76193; -.
DR PaxDb; P76193; -.
DR PRIDE; P76193; -.
DR EnsemblBacteria; AAC74748; AAC74748; b1678.
DR EnsemblBacteria; BAA15458; BAA15458; BAA15458.
DR GeneID; 946174; -.
DR KEGG; ecj:JW1668; -.
DR KEGG; eco:b1678; -.
DR PATRIC; fig|511145.12.peg.1749; -.
DR EchoBASE; EB3771; -.
DR eggNOG; COG1376; Bacteria.
DR HOGENOM; CLU_046834_0_0_6; -.
DR InParanoid; P76193; -.
DR OMA; LAEYRMY; -.
DR PhylomeDB; P76193; -.
DR BioCyc; EcoCyc:G6904-MON; -.
DR BioCyc; MetaCyc:G6904-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P76193; -.
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:0009252; P:peptidoglycan biosynthetic process; IDA:EcoCyc.
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; 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..334
FT /note="Probable L,D-transpeptidase YnhG"
FT /id="PRO_0000013855"
FT DOMAIN 40..84
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 303..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 209
FT /evidence="ECO:0000255"
SQ SEQUENCE 334 AA; 36082 MW; 25078BB429389D5F CRC64;
MKRASLLTLT LIGAFSAIQA AWAVDYPLPP TGSRLVGQNQ TYTVQEGDKN LQAIARRFDT
AAMLILEANN TIAPVPKPGT TITIPSQLLL PDAPRQGIIV NLAELRLYYY PPGENIVQVY
PIGIGLQGLE TPVMETRVGQ KIPNPTWTPT AGIRQRSLER GIKLPPVVPA GPNNPLGRYA
LRLAHGNGEY LIHGTSAPDS VGLRVSSGCI RMNAPDIKAL FSSVRTGTPV KVINEPVKYS
VEPNGMRYVE VHRPLSAEEQ QNVQTMPYTL PAGFTQFKDN KAVDQKLVDK ALYRRAGYPV
SVSSGATPAA SNAPSVESAQ NGEPEQGNML RVTQ
