ERFK_ECOLI
ID ERFK_ECOLI Reviewed; 310 AA.
AC P39176;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable L,D-transpeptidase ErfK/SrfK;
DE EC=2.-.-.-;
DE Flags: Precursor;
GN Name=erfK; Synonyms=yeeG, yzzT; OrderedLocusNames=b1990, JW1968;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7592411; DOI=10.1128/jb.177.22.6371-6380.1995;
RA Lawrence J.G., Roth J.R.;
RT "The cobalamin (coenzyme B12) biosynthetic genes of Escherichia coli.";
RL J. Bacteriol. 177:6371-6380(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 22-33.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
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 [7]
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 -!- INTERACTION:
CC P39176; P08312: pheS; NbExp=4; IntAct=EBI-555707, EBI-555676;
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, also known as the Braun lipoprotein) to the
CC peptidoglycan. Complementation with erfK restores some of this
CC anchoring. {ECO:0000269|PubMed:18456808}.
CC -!- SIMILARITY: Belongs to the YkuD family. {ECO:0000305}.
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DR EMBL; U33333; AAA78909.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75051.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15807.1; -; Genomic_DNA.
DR PIR; E64963; E64963.
DR RefSeq; NP_416494.1; NC_000913.3.
DR AlphaFoldDB; P39176; -.
DR SMR; P39176; -.
DR BioGRID; 4259382; 19.
DR BioGRID; 849652; 1.
DR DIP; DIP-9522N; -.
DR IntAct; P39176; 3.
DR STRING; 511145.b1990; -.
DR MEROPS; C82.A02; -.
DR jPOST; P39176; -.
DR PaxDb; P39176; -.
DR PRIDE; P39176; -.
DR EnsemblBacteria; AAC75051; AAC75051; b1990.
DR EnsemblBacteria; BAA15807; BAA15807; BAA15807.
DR GeneID; 945273; -.
DR KEGG; ecj:JW1968; -.
DR KEGG; eco:b1990; -.
DR PATRIC; fig|511145.12.peg.2065; -.
DR EchoBASE; EB2546; -.
DR eggNOG; COG1376; Bacteria.
DR HOGENOM; CLU_046834_0_1_6; -.
DR InParanoid; P39176; -.
DR OMA; KQEGPTW; -.
DR PhylomeDB; P39176; -.
DR BioCyc; EcoCyc:G7073-MON; -.
DR BioCyc; MetaCyc:G7073-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P39176; -.
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; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Glycosyltransferase; Hydrolase; Peptidoglycan synthesis; Periplasm;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 22..310
FT /note="Probable L,D-transpeptidase ErfK/SrfK"
FT /id="PRO_0000021194"
FT ACT_SITE 207
FT /evidence="ECO:0000255"
FT CONFLICT 28..29
FT /note="PE -> TD (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 34411 MW; ABF26AC3E6F550AB CRC64;
MRRVNILCSF ALLFASHTSL AVTYPLPPEG SRLVGQSFTV TVPDHNTQPL ETFAAQYGQG
LSNMLEANPG ADVFLPKSGS QLTIPQQLIL PDTVRKGIVV NVAEMRLYYY PPDSNTVEVF
PIGIGQAGRE TPRNWVTTVE RKQEAPTWTP TPNTRREYAK RGESLPAFVP AGPDNPMGLY
AIYIGRLYAI HGTNANFGIG LRVSQGCIRL RNDDIKYLFD NVPVGTRVQI IDQPVKYTTE
PDGSNWLEVH EPLSRNRAEY ESDRKVPLPV TPSLRAFING QEVDVNRANA ALQRRSGMPV
QISSGSRQMF
