LPOA_ECOLI
ID LPOA_ECOLI Reviewed; 678 AA.
AC P45464; Q2M963;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Penicillin-binding protein activator LpoA;
DE Short=PBP activator LpoA;
DE AltName: Full=Lipoprotein activator of PBP from the outer membrane A;
DE Flags: Precursor;
GN Name=lpoA; Synonyms=yraM; OrderedLocusNames=b3147, JW3116;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP FUNCTION, INTERACTION WITH PBP1A, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=21183073; DOI=10.1016/j.cell.2010.11.038;
RA Typas A., Banzhaf M., van den Berg van Saparoea B., Verheul J., Biboy J.,
RA Nichols R.J., Zietek M., Beilharz K., Kannenberg K., von Rechenberg M.,
RA Breukink E., den Blaauwen T., Gross C.A., Vollmer W.;
RT "Regulation of peptidoglycan synthesis by outer-membrane proteins.";
RL Cell 143:1097-1109(2010).
RN [4]
RP FUNCTION, INTERACTION WITH PBP1A, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21183074; DOI=10.1016/j.cell.2010.11.037;
RA Paradis-Bleau C., Markovski M., Uehara T., Lupoli T.J., Walker S.,
RA Kahne D.E., Bernhardt T.G.;
RT "Lipoprotein cofactors located in the outer membrane activate bacterial
RT cell wall polymerases.";
RL Cell 143:1110-1120(2010).
CC -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential for
CC the function of penicillin-binding protein 1A (PBP1a). Stimulates
CC transpeptidase activity of PBP1a in vitro.
CC {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}.
CC -!- SUBUNIT: Interacts with PBP1a. {ECO:0000269|PubMed:21183073,
CC ECO:0000269|PubMed:21183074}.
CC -!- INTERACTION:
CC P45464; P16433: hycG; NbExp=2; IntAct=EBI-557795, EBI-541977;
CC P45464; P02918: mrcA; NbExp=4; IntAct=EBI-557795, EBI-1126191;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:21183073,
CC ECO:0000269|PubMed:21183074}; Lipid-anchor
CC {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}; Periplasmic
CC side {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}.
CC Note=Localizes at the sidewall of elongating cells.
CC -!- DISRUPTION PHENOTYPE: Absence of both LpoA and LpoB leads to a decrease
CC in peptide cross-linking and to cell lysis.
CC {ECO:0000269|PubMed:21183074}.
CC -!- SIMILARITY: Belongs to the LpoA family. {ECO:0000305}.
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DR EMBL; U18997; AAA57950.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76181.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77193.1; -; Genomic_DNA.
DR PIR; G65104; G65104.
DR RefSeq; NP_417616.1; NC_000913.3.
DR RefSeq; WP_000249104.1; NZ_LN832404.1.
DR PDB; 2MHK; NMR; -; A=28-256.
DR PDB; 6DR3; X-ray; 2.10 A; A=31-252.
DR PDBsum; 2MHK; -.
DR PDBsum; 6DR3; -.
DR AlphaFoldDB; P45464; -.
DR BMRB; P45464; -.
DR SMR; P45464; -.
DR BioGRID; 4261989; 57.
DR DIP; DIP-12897N; -.
DR IntAct; P45464; 4.
DR STRING; 511145.b3147; -.
DR jPOST; P45464; -.
DR PaxDb; P45464; -.
DR PRIDE; P45464; -.
DR EnsemblBacteria; AAC76181; AAC76181; b3147.
DR EnsemblBacteria; BAE77193; BAE77193; BAE77193.
DR GeneID; 947663; -.
DR KEGG; ecj:JW3116; -.
DR KEGG; eco:b3147; -.
DR PATRIC; fig|511145.12.peg.3242; -.
DR EchoBASE; EB2631; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_1_6; -.
DR InParanoid; P45464; -.
DR OMA; MRLYAMG; -.
DR PhylomeDB; P45464; -.
DR BioCyc; EcoCyc:G7642-MON; -.
DR BioCyc; MetaCyc:G7642-MON; -.
DR PRO; PR:P45464; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0031241; C:periplasmic side of cell outer membrane; IDA:UniProtKB.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:UniProtKB.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR HAMAP; MF_01890; LpoA; 1.
DR InterPro; IPR007443; LpoA.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR38038; PTHR38038; 1.
DR Pfam; PF04348; LppC; 1.
DR SUPFAM; SSF48435; SSF48435; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell shape; Lipoprotein; Membrane;
KW Palmitate; Peptidoglycan synthesis; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..678
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000169452"
FT REGION 302..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:6DR3"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:6DR3"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:2MHK"
SQ SEQUENCE 678 AA; 72825 MW; 1A724681E3BEA433 CRC64;
MVPSTFSRLK AARCLPVVLA ALIFAGCGTH TPDQSTAYMQ GTAQADSAFY LQQMQQSSDD
TRINWQLLAI RALVKEGKTG QAVELFNQLP QELNDAQRRE KTLLAVEIKL AQKDFAGAQN
LLAKITPADL EQNQQARYWQ AKIDASQGRP SIDLLRALIA QEPLLGAKEK QQNIDATWQA
LSSMTQEQAN TLVINADENI LQGWLDLQRV WFDNRNDPDM MKAGIADWQK RYPNNPGAKM
LPTQLVNVKA FKPASTNKIA LLLPLNGQAA VFGRTIQQGF EAAKNIGTQP VAAQVAAAPA
ADVAEQPQPQ TVDGVASPAQ ASVSDLTGEQ PAAQPVPVSA PATSTAAVSA PANPSAELKI
YDTSSQPLSQ ILSQVQQDGA SIVVGPLLKN NVEELLKSNT PLNVLALNQP ENIENRVNIC
YFALSPEDEA RDAARHIRDQ GKQAPLVLIP RSSLGDRVAN AFAQEWQKLG GGTVLQQKFG
STSELRAGVN GGSGIALTGS PITLRATTDS GMTTNNPTLQ TTPTDDQFTN NGGRVDAVYI
VATPGEIAFI KPMIAMRNGS QSGATLYASS RSAQGTAGPD FRLEMEGLQY SEIPMLAGGN
LPLMQQALSA VNNDYSLARM YAMGVDAWSL ANHFSQMRQV QGFEINGNTG SLTANPDCVI
NRNLSWLQYQ QGQVVPVS
