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 03-AUG-2022, entry version 125.
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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Lytic transglycosylase with a strong preference for naked
CC glycan strands that lack stem peptides. {ECO:0000255|HAMAP-
CC Rule:MF_02071}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02071};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_02071}.
CC -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000255|HAMAP-
CC Rule:MF_02071}.
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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_SWKA01000005.1.
DR AlphaFoldDB; Q8XBQ1; -.
DR SMR; Q8XBQ1; -.
DR STRING; 155864.EDL933_0707; -.
DR PRIDE; Q8XBQ1; -.
DR EnsemblBacteria; AAG54967; AAG54967; Z0778.
DR EnsemblBacteria; BAB34094; BAB34094; ECs_0671.
DR GeneID; 917032; -.
DR KEGG; ece:Z0778; -.
DR KEGG; ecs:ECs_0671; -.
DR PATRIC; fig|386585.9.peg.783; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_3_0_6; -.
DR OMA; PFYSDRI; -.
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:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:UniProtKB-UniRule.
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; IPR036908; RlpA-like_sf.
DR InterPro; IPR012997; RplA.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
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;
KW Cell membrane; Cell wall biogenesis/degradation; Lipoprotein; Lyase;
KW Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT CHAIN 18..362
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT /id="PRO_0000030797"
FT DOMAIN 285..361
FT /note="SPOR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT REGION 198..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="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
