(data stored in ACNUC7421 zone)

SWISSPROT: RLPA_ECO57

ID   RLPA_ECO57              Reviewed;         362 AA.
AC   Q8XBQ1;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 105.
DE   RecName: Full=Endolytic peptidoglycan transglycosylase RlpA {ECO:0000255|HAMAP-Rule:MF_02071};
DE            EC=4.2.2.- {ECO:0000255|HAMAP-Rule:MF_02071};
DE   AltName: Full=Rare lipoprotein A;
DE   Flags: Precursor;
GN   Name=rlpA {ECO:0000255|HAMAP-Rule:MF_02071};
GN   OrderedLocusNames=Z0778, ECs0671;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Lytic transglycosylase with a strong preference for
CC       naked glycan strands that lack stem peptides. {ECO:0000255|HAMAP-
CC       Rule:MF_02071}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02071}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_02071}.
CC   -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_02071}.
DR   EMBL; AE005174; AAG54967.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34094.1; -; Genomic_DNA.
DR   PIR; C85563; C85563.
DR   PIR; G90712; G90712.
DR   RefSeq; NP_308698.1; NC_002695.1.
DR   RefSeq; WP_001231402.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; Q8XBQ1; -.
DR   SMR; Q8XBQ1; -.
DR   STRING; 155864.Z0778; -.
DR   EnsemblBacteria; AAG54967; AAG54967; Z0778.
DR   EnsemblBacteria; BAB34094; BAB34094; BAB34094.
DR   GeneID; 917032; -.
DR   KEGG; ece:Z0778; -.
DR   KEGG; ecs:ECs0671; -.
DR   PATRIC; fig|386585.9.peg.783; -.
DR   eggNOG; ENOG4105K6T; Bacteria.
DR   eggNOG; COG0797; LUCA.
DR   HOGENOM; HOG000117956; -.
DR   KO; K03642; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.40.10; -; 1.
DR   Gene3D; 3.30.70.1070; -; 1.
DR   HAMAP; MF_02071; RlpA; 1.
DR   InterPro; IPR034718; RlpA.
DR   InterPro; IPR009009; RlpA-like_DPBB.
DR   InterPro; IPR012997; RplA.
DR   InterPro; IPR007730; SPOR_dom.
DR   Pfam; PF03330; DPBB_1; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF110997; SSF110997; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   TIGRFAMs; TIGR00413; rlpA; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8XBQ1.
DR   SWISS-2DPAGE; Q8XBQ1.
KW   Cell membrane; Cell wall biogenesis/degradation; Complete proteome;
KW   Lipoprotein; Lyase; Membrane; Palmitate; Signal.
FT   SIGNAL        1     17       {ECO:0000255|HAMAP-Rule:MF_02071}.
FT   CHAIN        18    362       Endolytic peptidoglycan transglycosylase
FT                                RlpA. {ECO:0000255|HAMAP-Rule:MF_02071}.
FT                                /FTId=PRO_0000030797.
FT   DOMAIN      285    361       SPOR. {ECO:0000255|HAMAP-Rule:MF_02071}.
FT   LIPID        18     18       N-palmitoyl cysteine. {ECO:0000255|HAMAP-
FT                                Rule:MF_02071}.
FT   LIPID        18     18       S-diacylglycerol cysteine.
FT                                {ECO:0000255|HAMAP-Rule:MF_02071}.
SQ   SEQUENCE   362 AA;  37553 MW;  24F37652DD3C1F46 CRC64;
     MRKQWLGICI AAGMLAACTS DDGQQQTVSV PQPAVCNGPI VEISGADPRF EPLNATANQD
     YQRDGKSYKI VQDPSRFIQA GLAAIYDAEP GSNLTASGEA FDPTQLTAAH PTLPIPSYAR
     ITNLANGRMI VVRINDRGPY GNDRVISLSR AAADRLNTSN NTKVRIDPII VAQDGSLSGP
     GMACTTVAKQ TYALPAPPDL SGGAGTSSVS GPQGDILPVS NSTLKSEDPT GAPVTSSGFL
     GAPTTLAPGV LEGSEPTPAP QPVVTAPSTT PATSPAMVTP QAASQSASGN FMVQVGAVSD
     QARAQQYQQQ LGQKFGVPGR VTQNGAVWRI QLGPFANKAE ASTLQQRLQT EAQLQSFITT
     AQ
//

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