RLPA_PSEAB
ID RLPA_PSEAB Reviewed; 341 AA.
AC A0A0H2ZFV1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Endolytic peptidoglycan transglycosylase RlpA {ECO:0000255|HAMAP-Rule:MF_02071, ECO:0000305};
DE EC=4.2.2.- {ECO:0000255|HAMAP-Rule:MF_02071, ECO:0000269|PubMed:24806796};
DE AltName: Full=Rare lipoprotein A {ECO:0000303|PubMed:24806796};
DE Flags: Precursor;
GN Name=rlpA {ECO:0000255|HAMAP-Rule:MF_02071, ECO:0000303|PubMed:24806796};
GN OrderedLocusNames=PA14_12090 {ECO:0000312|EMBL:ABJ13274.1};
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLU-120; ASP-123; HIS-131 AND ASP-157.
RX PubMed=24806796; DOI=10.1111/mmi.12643;
RA Jorgenson M.A., Chen Y., Yahashiri A., Popham D.L., Weiss D.S.;
RT "The bacterial septal ring protein RlpA is a lytic transglycosylase that
RT contributes to rod shape and daughter cell separation in Pseudomonas
RT aeruginosa.";
RL Mol. Microbiol. 93:113-128(2014).
CC -!- FUNCTION: Lytic transglycosylase with a strong preference for naked
CC glycan strands that lack stem peptides. Required for efficient
CC separation of daughter cells and maintenance of rod shape.
CC {ECO:0000269|PubMed:24806796}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02071};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_02071}. Note=Localizes at the
CC septal ring. {ECO:0000269|PubMed:24806796}.
CC -!- DOMAIN: The SPOR domain is important for normal localization, but not
CC for cell division or rod shape. {ECO:0000269|PubMed:24806796}.
CC -!- DISRUPTION PHENOTYPE: Mutants form chains of short, fat cells when
CC grown in low osmotic strength media. {ECO:0000269|PubMed:24806796}.
CC -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000255|HAMAP-
CC Rule:MF_02071}.
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DR EMBL; CP000438; ABJ13274.1; -; Genomic_DNA.
DR RefSeq; WP_003093184.1; NZ_CP034244.1.
DR AlphaFoldDB; A0A0H2ZFV1; -.
DR SMR; A0A0H2ZFV1; -.
DR EnsemblBacteria; ABJ13274; ABJ13274; PA14_12090.
DR KEGG; pau:PA14_12090; -.
DR HOGENOM; CLU_042923_3_2_6; -.
DR OMA; PFYSDRI; -.
DR BioCyc; PAER208963:G1G74-1004-MON; -.
DR Proteomes; UP000000653; 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 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Lipoprotein; Lyase;
KW Membrane; Palmitate; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT CHAIN 27..341
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /id="PRO_5002603392"
FT DOMAIN 260..341
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 MUTAGEN 120
FT /note="E->A: Strong decrease in transglycosylase activity."
FT /evidence="ECO:0000269|PubMed:24806796"
FT MUTAGEN 123
FT /note="D->A: Strong decrease in transglycosylase activity."
FT /evidence="ECO:0000269|PubMed:24806796"
FT MUTAGEN 131
FT /note="H->A: Strong decrease in transglycosylase activity."
FT /evidence="ECO:0000269|PubMed:24806796"
FT MUTAGEN 157
FT /note="D->N: Lack of transglycosylase activity."
FT /evidence="ECO:0000269|PubMed:24806796"
SQ SEQUENCE 341 AA; 36442 MW; CC6122366C86D9A5 CRC64;
MSKRVRSSLI LPAVCGLGLA AVLLSSCSSK APQQPARQAG ISGPGDYSRP HRDGAPWWDV
DVSRIPDAVP MPHNGSVKAN PYTVLGKTYY PMNDARAYRM VGTASWYGTK FHGQATANGE
TYDLYGMTAA HKTLPLPSYV RVTNLDNGKS VIVRVNDRGP FYSDRVIDLS FAAAKKLGYA
ETGTARVKVE GIDPVQWWAQ RGRPAPMVLA QPKQAVAQAP AATQTQAVAM AQPIETYTPP
PAQHAAAVLP VQIDSKKNAS LPADGLYLQV GAFANPDAAE LLKAKLSGVT AAPVFISSVV
RNQQILHRVR LGPIGSADEV SRTQDSIRVA NLGQPTLVRP D
