RLPA_SALTI
ID RLPA_SALTI Reviewed; 377 AA.
AC Q8Z8I0;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 127.
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};
GN OrderedLocusNames=STY0689, t2229;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD05115.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69832.1; -; Genomic_DNA.
DR RefSeq; NP_455214.1; NC_003198.1.
DR RefSeq; WP_000549517.1; NZ_WSUR01000015.1.
DR AlphaFoldDB; Q8Z8I0; -.
DR SMR; Q8Z8I0; -.
DR STRING; 220341.16501889; -.
DR EnsemblBacteria; AAO69832; AAO69832; t2229.
DR KEGG; stt:t2229; -.
DR KEGG; sty:STY0689; -.
DR PATRIC; fig|220341.7.peg.692; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_3_0_6; -.
DR OMA; PFYSDRI; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
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; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT CHAIN 20..377
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT /id="PRO_0000030798"
FT DOMAIN 300..376
FT /note="SPOR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT REGION 196..277
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 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 377 AA; 38769 MW; 41D73D3D9C6FD68B CRC64;
MHKQLPVICV AAGIVLLAAC TNDGGQQQTT VAPQPAVCNG PTVEISGAEP RYEPLNPTAN
QDYQRDGKSY KIVQDPSRFS QAGLAAIYDA EPGSNLTASG EMFDPMQLTA AHPTLPIPSY
ARITNLANGR MIVVRINDRG LYGTDRVISL SRAAADRLNT SNNTKVRIDP IIVAPDGSLS
GPGMACTTVA KQTYALPPRP DLSGGMGSAS SAPAQPQGDV LPVSNSTLKS DDTTGAPVSS
SGFLGAPTTL APGVLEGNEP TPAPQTAPVS APVTAPATAT PVSAPAAAAP VSAPVSAPAA
AASGRFVVQV GAVSDQTRAQ QYQQRLSQQF SVPGRVIQNG AVWRIQLGPF ASKAEASALQ
QRLQTEAQLQ SFIASAQ
