(data stored in SCRATCH zone)

SWISSPROT: C8U2Z5_ECO10

ID   C8U2Z5_ECO10            Unreviewed;       362 AA.
AC   C8U2Z5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 52.
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:BAI29503.1};
GN   OrderedLocusNames=ECO103_0640 {ECO:0000313|EMBL:BAI29503.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29503.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29503.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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; AP010958; BAI29503.1; -; Genomic_DNA.
DR   RefSeq; WP_001231428.1; NC_013353.1.
DR   SMR; C8U2Z5; -.
DR   EnsemblBacteria; BAI29503; BAI29503; ECO103_0640.
DR   KEGG; eoh:ECO103_0640; -.
DR   HOGENOM; HOG000117956; -.
DR   KO; K03642; -.
DR   OMA; PFYSDRI; -.
DR   BioCyc; ECOL585395:ECO103_RS03340-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U2Z5.
DR   SWISS-2DPAGE; C8U2Z5.
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02071};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Lipoprotein {ECO:0000313|EMBL:BAI29503.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_02071}.
FT   DOMAIN      285    361       SPOR. {ECO:0000259|PROSITE:PS51724}.
SQ   SEQUENCE   362 AA;  37500 MW;  2D6C1FADDBA15694 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 QPVVTAPSTT PATSPAMVTP QAASQSASGN FMVQVGAVSD
     QARAQQYQQQ LGQKFGVPGR VTQNGAVWRI QLGPFASKAE ASTLQQRLQT EAQLQSFITT
     AQ
//

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