RLPA_PSEAE
ID RLPA_PSEAE Reviewed; 342 AA.
AC Q9X6V6;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
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}; OrderedLocusNames=PA4000;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Gagnon L.A., Castro-Urbina I.M., Liao X., Hancock R.E.W., Clarke A.J.,
RA Huletsky A.;
RT "Cloning and characterization of PBP5 of Pseudomonas aeruginosa.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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; AF147448; AAD32233.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07387.1; -; Genomic_DNA.
DR PIR; D83146; D83146.
DR RefSeq; NP_252689.1; NC_002516.2.
DR RefSeq; WP_003100310.1; NZ_QZGE01000038.1.
DR PDB; 6I05; X-ray; 1.21 A; A=264-342.
DR PDB; 6I09; X-ray; 1.48 A; A=265-342.
DR PDB; 6I0A; X-ray; 1.30 A; A=266-342.
DR PDB; 6I0N; X-ray; 1.40 A; A=266-342.
DR PDBsum; 6I05; -.
DR PDBsum; 6I09; -.
DR PDBsum; 6I0A; -.
DR PDBsum; 6I0N; -.
DR AlphaFoldDB; Q9X6V6; -.
DR SMR; Q9X6V6; -.
DR STRING; 287.DR97_3867; -.
DR PaxDb; Q9X6V6; -.
DR PRIDE; Q9X6V6; -.
DR EnsemblBacteria; AAG07387; AAG07387; PA4000.
DR GeneID; 878957; -.
DR KEGG; pae:PA4000; -.
DR PATRIC; fig|208964.12.peg.4192; -.
DR PseudoCAP; PA4000; -.
DR HOGENOM; CLU_042923_3_2_6; -.
DR InParanoid; Q9X6V6; -.
DR OMA; PFYSDRI; -.
DR PhylomeDB; Q9X6V6; -.
DR BioCyc; PAER208964:G1FZ6-4073-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation; Lipoprotein;
KW Lyase; Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT CHAIN 27..342
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT /id="PRO_0000030809"
FT DOMAIN 261..342
FT /note="SPOR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
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"
FT STRAND 267..276
FT /evidence="ECO:0007829|PDB:6I05"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:6I05"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:6I05"
FT STRAND 305..316
FT /evidence="ECO:0007829|PDB:6I05"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:6I05"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6I05"
SQ SEQUENCE 342 AA; 36483 MW; 18D08C614B23E24D CRC64;
MSKRVRSSLI LPAVCGLGLA AVLLSSCSSK APQQPARQAG ISGPGDYSRP HRDGAPWWDV
DVSRIPDAVP MPHNGSVKAN PYTVLGKTYY PMNDARAYRM VGTASWYGTK FHGQATANGE
TYDLYGMTAA HKTLPLPSYV RVTNLDNGKS VIVRVNDRGP FYSDRVIDLS FAAAKKLGYA
ETGTARVKVE GIDPVQWWAQ RGRPAPMVLA QPKQAVAQAA PAAAQTQAVA MAQPIETYTP
PPAQHAAAVL PVQIDSKKNA SLPADGLYLQ VGAFANPDAA ELLKAKLSGV TAAPVFISSV
VRNQQILHRV RLGPIGSADE VSRTQDSIRV ANLGQPTLVR PD
