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Database: UniProt
Entry: A7H4G6_CAMJD
LinkDB: A7H4G6_CAMJD
Original site: A7H4G6_CAMJD 
ID   A7H4G6_CAMJD            Unreviewed;       275 AA.
AC   A7H4G6;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Probable endolytic peptidoglycan transglycosylase RlpA {ECO:0000256|HAMAP-Rule:MF_02071};
DE            EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02071};
GN   Name=rlpA {ECO:0000256|HAMAP-Rule:MF_02071,
GN   ECO:0000313|EMBL:ABS44355.1};
GN   OrderedLocusNames=JJD26997_1353 {ECO:0000313|EMBL:ABS44355.1};
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109 {ECO:0000313|EMBL:ABS44355.1, ECO:0000313|Proteomes:UP000002302};
RN   [1] {ECO:0000313|Proteomes:UP000002302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97
RC   {ECO:0000313|Proteomes:UP000002302};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lytic transglycosylase with a strong preference for naked
CC       glycan strands that lack stem peptides. {ECO:0000256|HAMAP-
CC       Rule:MF_02071}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02071};
CC       Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_02071}.
CC   -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_02071, ECO:0000256|RuleBase:RU003495}.
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DR   EMBL; CP000768; ABS44355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H4G6; -.
DR   SMR; A7H4G6; -.
DR   KEGG; cjd:JJD26997_1353; -.
DR   HOGENOM; CLU_042923_3_4_7; -.
DR   Proteomes; UP000002302; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   CDD; cd22268; DPBB_RlpA-like; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   Gene3D; 3.30.70.1070; Sporulation related repeat; 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   NCBIfam; TIGR00413; rlpA; 1.
DR   PANTHER; PTHR34183; -; 1.
DR   PANTHER; PTHR34183:SF1; ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA; 1.
DR   Pfam; PF03330; DPBB_1; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF110997; Sporulation related repeat; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02071};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02071};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW   Rule:MF_02071};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_02071};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..275
FT                   /note="Probable endolytic peptidoglycan transglycosylase
FT                   RlpA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009990706"
FT   DOMAIN          200..275
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
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
//
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