(data stored in SCRATCH zone)

SWISSPROT: B7UKS3_ECO27

ID   B7UKS3_ECO27            Unreviewed;       362 AA.
AC   B7UKS3;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 50.
DE   RecName: Full=Endolytic peptidoglycan transglycosylase RlpA {ECO:0000256|HAMAP-Rule:MF_02071};
DE            EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02071};
GN   Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071,
GN   ECO:0000313|EMBL:CAS08081.1};
GN   OrderedLocusNames=E2348C_0533 {ECO:0000313|EMBL:CAS08081.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08081.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08081.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Lytic transglycosylase with a strong preference for
CC       naked glycan strands that lack stem peptides. {ECO:0000256|HAMAP-
CC       Rule:MF_02071}.
CC   -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_02071, ECO:0000256|RuleBase:RU003495}.
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DR   EMBL; FM180568; CAS08081.1; -; Genomic_DNA.
DR   RefSeq; WP_001231425.1; NC_011601.1.
DR   EnsemblBacteria; CAS08081; CAS08081; E2348C_0533.
DR   KEGG; ecg:E2348C_0533; -.
DR   HOGENOM; HOG000117956; -.
DR   KO; K03642; -.
DR   OMA; PFYSDRI; -.
DR   BioCyc; ECOL574521:E2348C_RS02805-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
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; PS51724; SPOR; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKS3.
DR   SWISS-2DPAGE; B7UKS3.
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02071};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Lipoprotein {ECO:0000313|EMBL:CAS08081.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_02071}.
FT   DOMAIN      285    361       SPOR. {ECO:0000259|PROSITE:PS51724}.
SQ   SEQUENCE   362 AA;  37514 MW;  F75D8CBE7022EEAF CRC64;
     MRKQWLGICI AAGMLAACTS DDGQQQTVSV PQPAVCNGPI VEISGADPRF EPLNATANQD
     YQRDGKSYKI VQDPSRFSQA GLAAIYDAEP GSNLTASGEA FDPTQLTAAH PTLPIPSYAR
     ITNLANGRMI VVRINDRGPY GNDRVISLSR AAADRLNTSN NTKVRIDPII VAQDGSLSGP
     GMACTTVAKQ TYALPAPPDL SGGAGTSSVS GPQGDILPVS NSTLKSEDPT GAPVTSSGFL
     GAPTTLAPGV LEGSEPTPAP QPIVTAPSTT PATSPAMVTP QAASQSASGN FMVQVGAVSD
     QARAQQYQQQ LGQKFGVPGR VTQNGAVWRI QLGPFASKAE ASTLQQRLQT EAQLQSFITT
     AQ
//

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