RLPA_ECOLI
ID RLPA_ECOLI Reviewed; 362 AA.
AC P10100;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 166.
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 {ECO:0000303|PubMed:3316191};
DE Flags: Precursor;
GN Name=rlpA {ECO:0000255|HAMAP-Rule:MF_02071, ECO:0000303|PubMed:3316191};
GN OrderedLocusNames=b0633, JW0628;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL AT CYS-18, PALMITOYLATION
RP AT CYS-18, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=3316191; DOI=10.1128/jb.169.12.5692-5699.1987;
RA Takase I., Ishino F., Wachi M., Kamata H., Doi M., Asoh S., Matsuzawa H.,
RA Ohta T., Matsuhashi M.;
RT "Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia
RT coli chromosome.";
RL J. Bacteriol. 169:5692-5699(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RC STRAIN=K12;
RX PubMed=2644207; DOI=10.1128/jb.171.1.558-560.1989;
RA Matsuzawa H., Asoh S., Kunai K., Muraiso K., Takasuga A., Ohta T.;
RT "Nucleotide sequence of the rodA gene, responsible for the rod shape of
RT Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding
RT protein 2, constitute the rodA operon.";
RL J. Bacteriol. 171:558-560(1989).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19684127; DOI=10.1128/jb.00811-09;
RA Gerding M.A., Liu B., Bendezu F.O., Hale C.A., Bernhardt T.G.,
RA de Boer P.A.;
RT "Self-enhanced accumulation of FtsN at division sites and roles for other
RT proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell
RT constriction.";
RL J. Bacteriol. 191:7383-7401(2009).
RN [9]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=K12 / BW25113;
RX PubMed=19880599; DOI=10.1128/jb.01244-09;
RA Arends S.J., Williams K., Scott R.J., Rolong S., Popham D.L., Weiss D.S.;
RT "Discovery and characterization of three new Escherichia coli septal ring
RT proteins that contain a SPOR domain: DamX, DedD, and RlpA.";
RL J. Bacteriol. 192:242-255(2010).
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 ECO:0000305|PubMed:3316191}. Note=Localizes at the septal ring. Is also
CC associated with some other structures/complexes along the cell
CC cylinder. {ECO:0000269|PubMed:19684127, ECO:0000269|PubMed:19880599}.
CC -!- DOMAIN: The SPOR domain binds septal peptidoglycans and is required to
CC target RlpA to the septal ring. {ECO:0000269|PubMed:19880599}.
CC -!- DISRUPTION PHENOTYPE: Deletion does not result in any obvious growth or
CC division defects. {ECO:0000269|PubMed:19684127}.
CC -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000255|HAMAP-
CC Rule:MF_02071}.
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DR EMBL; M18276; AAA24552.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40833.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73734.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35276.1; -; Genomic_DNA.
DR EMBL; M22857; AAA24572.1; -; Genomic_DNA.
DR PIR; A28387; LPECRA.
DR RefSeq; NP_415166.1; NC_000913.3.
DR RefSeq; WP_001231430.1; NZ_SSZK01000037.1.
DR AlphaFoldDB; P10100; -.
DR SMR; P10100; -.
DR BioGRID; 4260680; 171.
DR BioGRID; 849624; 1.
DR IntAct; P10100; 1.
DR STRING; 511145.b0633; -.
DR jPOST; P10100; -.
DR PaxDb; P10100; -.
DR PRIDE; P10100; -.
DR EnsemblBacteria; AAC73734; AAC73734; b0633.
DR EnsemblBacteria; BAA35276; BAA35276; BAA35276.
DR GeneID; 945241; -.
DR KEGG; ecj:JW0628; -.
DR KEGG; eco:b0633; -.
DR PATRIC; fig|1411691.4.peg.1635; -.
DR EchoBASE; EB0847; -.
DR eggNOG; COG0797; Bacteria.
DR HOGENOM; CLU_042923_3_0_6; -.
DR InParanoid; P10100; -.
DR OMA; PFYSDRI; -.
DR PhylomeDB; P10100; -.
DR BioCyc; EcoCyc:EG10854-MON; -.
DR PRO; PR:P10100; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
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; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071,
FT ECO:0000305|PubMed:3316191"
FT CHAIN 18..362
FT /note="Endolytic peptidoglycan transglycosylase RlpA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT /id="PRO_0000030796"
FT DOMAIN 285..361
FT /note="SPOR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071"
FT REGION 198..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071,
FT ECO:0000269|PubMed:3316191"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02071,
FT ECO:0000269|PubMed:3316191"
SQ SEQUENCE 362 AA; 37528 MW; E28B57023CF15686 CRC64;
MRKQWLGICI AAGMLAACTS DDGQQQTVSV PQPAVCNGPI VEISGADPRF EPLNATANQD
YQRDGKSYKI VQDPSRFSQA GLAAIYDAEP GSNLTASGEA FDPTQLTAAH PTLPIPSYAR
ITNLANGRMI VVRINDRGPY GNDRVISLSR AAADRLNTSN NTKVRIDPII VAQDGSLSGP
GMACTTVAKQ TYALPAPPDL SGGAGTSSVS GPQGDILPVS NSTLKSEDPT GAPVTSSGFL
GAPTTLAPGV LEGSEPTPAP QPVVTAPSTT PATSPAMVTP QAVSQSASGN FMVQVGAVSD
QARAQQYQQQ LGQKFGVPGR VTQNGAVWRI QLGPFASKAE ASTLQQRLQT EAQLQSFITT
AQ
