RLPA_CAMJE
ID RLPA_CAMJE Reviewed; 275 AA.
AC Q9PHM1; Q0PAM2;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Flags: Precursor;
GN Name=rlpA {ECO:0000255|HAMAP-Rule:MF_02071}; OrderedLocusNames=Cj0646;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL34791.1; -; Genomic_DNA.
DR PIR; E81413; E81413.
DR RefSeq; WP_002852227.1; NC_002163.1.
DR RefSeq; YP_002344075.1; NC_002163.1.
DR AlphaFoldDB; Q9PHM1; -.
DR SMR; Q9PHM1; -.
DR IntAct; Q9PHM1; 2.
DR STRING; 192222.Cj0646; -.
DR PaxDb; Q9PHM1; -.
DR PRIDE; Q9PHM1; -.
DR DNASU; 904973; -.
DR EnsemblBacteria; CAL34791; CAL34791; Cj0646.
DR GeneID; 904973; -.
DR KEGG; cje:Cj0646; -.
DR PATRIC; fig|192222.6.peg.638; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_3_4_7; -.
DR OMA; MGAFRNQ; -.
DR Proteomes; UP000000799; 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; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT CHAIN 23..275
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT /id="PRO_0000030802"
FT DOMAIN 200..275
FT /note="SPOR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
SQ SEQUENCE 275 AA; 29375 MW; 8B506911ECEDE916 CRC64;
MQIKTITLKL SAVSLGALFF SGCLGTSFFS SLDNAQVYYP SNDFKSSPSS SGTKGTMKPY
TINGKTYYPT VVAVGETADG IASWYGPGFH GKKTSNGETY NQNALTAAHK TLPMNTILKV
TNLNNNRQVT VRVNDRGPFV NNRIIDLSKG AASQIDMIAS GTAPVRLEVI GFGSSNSGNN
IVHSNVNYGN SGEIANNGQI YEGGNFMVQI GAFKNPAGAQ TIAARYKTYR TYSSTIRTSS
VDGLNRVFLT GFRSEDEARD FAASGAFAGA FVVRE