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 27-MAR-2024, entry version 120.
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; Aquificota; 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 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 InParanoid; O67235; -.
DR OrthoDB; 9779128at2; -.
DR Proteomes; UP000000798; 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: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 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 NCBIfam; TIGR00413; rlpA; 1.
DR PANTHER; PTHR34183; -; 1.
DR PANTHER; PTHR34183:SF1; ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA; 1.
DR Pfam; PF03330; DPBB_1; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 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
//
