ID   RLPA_RICTY              Reviewed;         320 AA.
AC   Q68WY7;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Endolytic peptidoglycan transglycosylase RlpA {ECO:0000255|HAMAP-Rule:MF_02071};
DE            EC=4.2.2.- {ECO:0000255|HAMAP-Rule:MF_02071};
GN   Name=rlpA {ECO:0000255|HAMAP-Rule:MF_02071}; OrderedLocusNames=RT0378;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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   -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_02071}.
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DR   EMBL; AE017197; AAU03855.1; -; Genomic_DNA.
DR   RefSeq; WP_011190839.1; NC_006142.1.
DR   AlphaFoldDB; Q68WY7; -.
DR   SMR; Q68WY7; -.
DR   STRING; 257363.RT0378; -.
DR   EnsemblBacteria; AAU03855; AAU03855; RT0378.
DR   KEGG; rty:RT0378; -.
DR   eggNOG; COG0797; Bacteria.
DR   HOGENOM; CLU_042923_6_1_5; -.
DR   OMA; GKTYKPH; -.
DR   OrthoDB; 2027419at2; -.
DR   Proteomes; UP000000604; 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: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   HAMAP; MF_02071; RlpA; 1.
DR   InterPro; IPR034718; RlpA.
DR   InterPro; IPR009009; RlpA-like_DPBB.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   InterPro; IPR022438; RPE5.
DR   InterPro; IPR012997; RplA.
DR   Pfam; PF03330; DPBB_1; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   TIGRFAMs; TIGR00413; rlpA; 1.
DR   TIGRFAMs; TIGR03776; RPE5; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Lyase.
FT   CHAIN           1..320
FT                   /note="Endolytic peptidoglycan transglycosylase RlpA"
FT                   /id="PRO_0000280828"
SQ   SEQUENCE   320 AA;  37374 MW;  8B5CB69430BCA8A3 CRC64;
     MIIMRNYKFK LESLHQNQKV FRRCTVHSTV LHIISLHEDW STRLTYKLSL YYCKIKNCYT
     TFKFEKSNRS IITRAERIIN VQHLRRCKDI VDNFSGLISI LLVLIFCINL SGCNTSKRLA
     YDNKYSYKEL SKDDPHNLTY IGHYKVGKNY KIKGKIYKPY TPKYFTETGY ASWYGGRKDG
     FHGKKTANGD RFNRNLLTAA HKTLPLPCLV KVTNKANNKS VILMVNDRGP FKKNRIIDVS
     QKAAEILAFK NQGITKVRIE YLPNETEKFL KKINLKKTEN KIFANNYKES LFTKVTKNNQ
     CSINCHIKLV NLKYKLAVNP