ID   RLPA_RICPR              Reviewed;         320 AA.
AC   Q9ZDE1;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 92.
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=RP390;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235271; CAA14847.1; -; Genomic_DNA.
DR   PIR; E71696; E71696.
DR   RefSeq; NP_220771.1; NC_000963.1.
DR   RefSeq; WP_010886281.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDE1; -.
DR   SMR; Q9ZDE1; -.
DR   STRING; 272947.gene:17555470; -.
DR   EnsemblBacteria; CAA14847; CAA14847; CAA14847.
DR   GeneID; 57569515; -.
DR   KEGG; rpr:RP390; -.
DR   PATRIC; fig|272947.5.peg.402; -.
DR   eggNOG; COG0797; Bacteria.
DR   HOGENOM; CLU_042923_6_1_5; -.
DR   OrthoDB; 9779128at2; -.
DR   Proteomes; UP000002480; Chromosome.
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   CDD; cd22268; DPBB_RlpA-like; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 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   NCBIfam; TIGR00413; rlpA; 1.
DR   NCBIfam; TIGR03776; RPE5; 1.
DR   PANTHER; PTHR34183; -; 1.
DR   PANTHER; PTHR34183:SF1; ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA; 1.
DR   Pfam; PF03330; DPBB_1; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Lyase; Reference proteome.
FT   CHAIN           1..320
FT                   /note="Endolytic peptidoglycan transglycosylase RlpA"
FT                   /id="PRO_0000190006"
SQ   SEQUENCE   320 AA;  37353 MW;  DBBB0B1EF6B8B34A CRC64;
     MIIMRNYKFK LEPLKQCQEA FKRYTVHSTA LYIIALQANW SRRLIYKLSL YFCKIKNCYT
     TFKFEQSNRF IITKAERIIK IQHLIRFKDI VNNFISLINI LLVLIFCINL SGCNASKKLS
     YSNKYSYKEL SKDDPHNLTY IGHYKVGKNY KIKGKIYKPH TPKYFTETGY ASWYGGRKDG
     FHGKTTANGD RFNRNLLTAA HKTLPLPCLV KVTNKVNNKS VILMVNDRGP FKKNRIIDVS
     QKAAEILAFK NQGVTKVRIE YLPNETEKFL KKINLKKPEN KTFAKNHKKS LFTQITKNNQ
     CSINCHIKLV NLKYKLAVNP
//