ID   RLPA_AQUAE              Reviewed;         226 AA.
AC   O67235;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable 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=aq_1174;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(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   -!- 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; AE000657; AAC07192.1; -; Genomic_DNA.
DR   PIR; H70400; H70400.
DR   RefSeq; NP_213799.1; NC_000918.1.
DR   RefSeq; WP_010880737.1; NC_000918.1.
DR   AlphaFoldDB; O67235; -.
DR   SMR; O67235; -.
DR   STRING; 224324.aq_1174; -.
DR   PRIDE; O67235; -.
DR   EnsemblBacteria; AAC07192; AAC07192; aq_1174.
DR   KEGG; aae:aq_1174; -.
DR   PATRIC; fig|224324.8.peg.912; -.
DR   eggNOG; COG0797; Bacteria.
DR   HOGENOM; CLU_1299232_0_0_0; -.
DR   OMA; PERYAYL; -.
DR   OrthoDB; 2027419at2; -.
DR   Proteomes; UP000000798; 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: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   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   Pfam; PF03330; DPBB_1; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   TIGRFAMs; TIGR00413; rlpA; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Lipoprotein; Lyase;
KW   Membrane; Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   CHAIN           27..226
FT                   /note="Probable endolytic peptidoglycan transglycosylase
FT                   RlpA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT                   /id="PRO_0000030801"
FT   LIPID           27
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT   LIPID           27
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
SQ   SEQUENCE   226 AA;  25857 MW;  D598B321BDC9D2BA CRC64;
     MERFLGFRTP LGALGVVILL TLILSSCSVK TSYKEKGRVY NGKCPEYAKV WVHYCPTKYA
     YTDRYQHLSK VKIVNPRNGK SVKISLRLNK KVRGICLPKR LKKYLGKPFL GKVYLLRCGE
     NGVKKCPKYI RGYASWYGGK FHGRKTASGI RFNQHEYYAA HRYLPFGTLL EVKNLKNGRK
     VIVKVVDRGP YVRGRHLDLS YAAAKKLGMI RDGVIPFEAK VLRCGY