NLPD_ECOLI
ID NLPD_ECOLI Reviewed; 379 AA.
AC P0ADA3; P33648; Q2MA87;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Murein hydrolase activator NlpD;
DE Flags: Precursor;
GN Name=nlpD; OrderedLocusNames=b2742, JW2712;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL AT CYS-26, AND
RP PALMITOYLATION AT CYS-26.
RC STRAIN=MP180;
RX PubMed=8132457; DOI=10.1128/jb.176.6.1630-1638.1994;
RA Ichikawa J.K., Li C., Fu J.C., Clarke S.;
RT "A gene at 59 minutes on the Escherichia coli chromosome encodes a
RT lipoprotein with unusual amino acid repeat sequences.";
RL J. Bacteriol. 176:1630-1638(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-379.
RC STRAIN=K12 / DH1 / ATCC 33849 / DSM 4235 / NCIB 12045;
RX PubMed=8208244; DOI=10.1007/bf00284200;
RA Takayanagi Y., Tanaka K., Takahashi H.;
RT "Structure of the 5' upstream region and the regulation of the rpoS gene of
RT Escherichia coli.";
RL Mol. Gen. Genet. 243:525-531(1994).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / TB28;
RX PubMed=19525345; DOI=10.1128/jb.00505-09;
RA Uehara T., Dinh T., Bernhardt T.G.;
RT "LytM-domain factors are required for daughter cell separation and rapid
RT ampicillin-induced lysis in Escherichia coli.";
RL J. Bacteriol. 191:5094-5107(2009).
RN [6]
RP FUNCTION AS AN ACTIVATOR.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20300061; DOI=10.1038/emboj.2010.36;
RA Uehara T., Parzych K.R., Dinh T., Bernhardt T.G.;
RT "Daughter cell separation is controlled by cytokinetic ring-activated cell
RT wall hydrolysis.";
RL EMBO J. 29:1412-1422(2010).
CC -!- FUNCTION: Activator of the cell wall hydrolase AmiC. Required for
CC septal murein cleavage and daughter cell separation during cell
CC division. {ECO:0000269|PubMed:19525345, ECO:0000269|PubMed:20300061}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Localizes at the septal
CC ring. {ECO:0000269|PubMed:19525345}.
CC -!- DISRUPTION PHENOTYPE: Cells are shorter in a single mutant, double
CC envC-nlpD disruptions have defects in septation and cell separation and
CC form long filaments (8-fold longer). Cell length increase is more
CC exacerbated with a triple mepM (yebA) or ygeR disruption (15-fold
CC longer) and further yet by the quadruple disruption mutant (envC-nlpD-
CC mepM(yebA)-ygeR, over 21-fold longer). Quadruple mutants are less
CC sensitive to ampicillin lysis. {ECO:0000269|PubMed:19525345}.
CC -!- SIMILARITY: Belongs to the E.coli NlpD/Haemophilus LppB family.
CC {ECO:0000305}.
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DR EMBL; L07869; AAA17875.1; -; Unassigned_DNA.
DR EMBL; U29579; AAA69252.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75784.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76819.1; -; Genomic_DNA.
DR EMBL; D17549; BAA04487.1; -; Genomic_DNA.
DR PIR; B55522; B55522.
DR RefSeq; NP_417222.1; NC_000913.3.
DR RefSeq; WP_001272592.1; NZ_STEB01000027.1.
DR AlphaFoldDB; P0ADA3; -.
DR SMR; P0ADA3; -.
DR BioGRID; 4261894; 278.
DR DIP; DIP-48067N; -.
DR IntAct; P0ADA3; 4.
DR STRING; 511145.b2742; -.
DR SWISS-2DPAGE; P0ADA3; -.
DR jPOST; P0ADA3; -.
DR PaxDb; P0ADA3; -.
DR PRIDE; P0ADA3; -.
DR EnsemblBacteria; AAC75784; AAC75784; b2742.
DR EnsemblBacteria; BAE76819; BAE76819; BAE76819.
DR GeneID; 66673384; -.
DR GeneID; 947011; -.
DR KEGG; ecj:JW2712; -.
DR KEGG; eco:b2742; -.
DR PATRIC; fig|1411691.4.peg.3998; -.
DR EchoBASE; EB2034; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG4942; Bacteria.
DR HOGENOM; CLU_029425_0_1_6; -.
DR InParanoid; P0ADA3; -.
DR OMA; TMFLIAY; -.
DR PhylomeDB; P0ADA3; -.
DR BioCyc; EcoCyc:EG12111-MON; -.
DR BioCyc; MetaCyc:EG12111-MON; -.
DR PRO; PR:P0ADA3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoliWiki.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; IDA:EcoCyc.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:EcoCyc.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IBA:GO_Central.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 2.70.70.10; -; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR016047; Peptidase_M23.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Repeat; Signal.
FT SIGNAL 1..25
FT CHAIN 26..379
FT /note="Murein hydrolase activator NlpD"
FT /id="PRO_0000018029"
FT REPEAT 66..73
FT /note="1-1"
FT REPEAT 74..81
FT /note="1-2; approximate"
FT REPEAT 82..89
FT /note="1-3"
FT REPEAT 90..97
FT /note="1-4; approximate"
FT DOMAIN 121..165
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REPEAT 205..211
FT /note="2-1"
FT REPEAT 227..233
FT /note="2-2"
FT REPEAT 239..245
FT /note="2-3"
FT REPEAT 246..252
FT /note="2-4"
FT REGION 30..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..97
FT /note="4 X 8 AA tandem repeats of Q-Q-P-Q-I-Q-P-V"
FT REGION 205..252
FT /note="4 X 7 AA approximate repeats"
FT REGION 210..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:8132457"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:8132457"
FT CONFLICT 139
FT /note="G -> A (in Ref. 4; BAA04487)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 40149 MW; A8E6A2B8456105FE CRC64;
MSAGSPKFTV RRIAALSLVS LWLAGCSDTS NPPAPVSSVN GNAPANTNSG MLITPPPKMG
TTSTAQQPQI QPVQQPQIQA TQQPQIQPVQ PVAQQPVQME NGRIVYNRQY GNIPKGSYSG
STYTVKKGDT LFYIAWITGN DFRDLAQRNN IQAPYALNVG QTLQVGNASG TPITGGNAIT
QADAAEQGVV IKPAQNSTVA VASQPTITYS ESSGEQSANK MLPNNKPTAT TVTAPVTVPT
ASTTEPTVSS TSTSTPISTW RWPTEGKVIE TFGASEGGNK GIDIAGSKGQ AIIATADGRV
VYAGNALRGY GNLIIIKHND DYLSAYAHND TMLVREQQEV KAGQKIATMG STGTSSTRLH
FEIRYKGKSV NPLRYLPQR
