ID   RLPA_SALTY              Reviewed;         381 AA.
AC   Q8ZR01;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
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}; OrderedLocusNames=STM0638;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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; AE006468; AAL19589.1; -; Genomic_DNA.
DR   RefSeq; NP_459630.1; NC_003197.2.
DR   RefSeq; WP_001231300.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZR01; -.
DR   SMR; Q8ZR01; -.
DR   STRING; 99287.STM0638; -.
DR   PaxDb; Q8ZR01; -.
DR   EnsemblBacteria; AAL19589; AAL19589; STM0638.
DR   GeneID; 1252158; -.
DR   KEGG; stm:STM0638; -.
DR   PATRIC; fig|99287.12.peg.673; -.
DR   HOGENOM; CLU_042923_3_0_6; -.
DR   OMA; PFYSDRI; -.
DR   PhylomeDB; Q8ZR01; -.
DR   BioCyc; SENT99287:STM0638-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   CHAIN           20..381
FT                   /note="Endolytic peptidoglycan transglycosylase RlpA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT                   /id="PRO_0000030799"
FT   DOMAIN          304..380
FT                   /note="SPOR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   REGION          196..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..273
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
SQ   SEQUENCE   381 AA;  39108 MW;  5B98C9876CAB14AF CRC64;
     MRKQLPVICV AAGIVLLAAC TNDGGQQQTT VAPQPAVCNG PTVEISGAEP RYEPLNPTAN
     QDYQRDGKSY KIVQDPSRFS QAGLAAIYDA EPGSNLTASG EMFDPMQLTA AHPTLPIPSY
     ARITNLANGR MIVVRINDRG PYGTDRVISL SRAAADRLNT SNNTKVRIDP IIVAPDGSLS
     GPGMACTTVA KQTYALPPRP DLSGGMGSAS SAPAQPQGDV LPVSNSTLKS DDTTGAPVSS
     SGFLGAPTTL APGVLESNEP TPAPQPAPVS APVAAPATAP ATATPVSAPA AAAPVSAPVS
     APAAAASGRF VVQVGAVSDQ TRAQQYQQRL SQQFSVPGRV IQNGAVWRIQ LGPFASKAEA
     SALQQRLQTE AQLQSFIASA Q