ID   LPOA_ECOL6              Reviewed;         678 AA.
AC   Q8FDA1;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Penicillin-binding protein activator LpoA {ECO:0000255|HAMAP-Rule:MF_01890};
DE            Short=PBP activator LpoA {ECO:0000255|HAMAP-Rule:MF_01890};
DE   Flags: Precursor;
GN   Name=lpoA {ECO:0000255|HAMAP-Rule:MF_01890}; OrderedLocusNames=c3900;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential for
CC       the function of penicillin-binding protein 1A (PBP1a).
CC       {ECO:0000255|HAMAP-Rule:MF_01890}.
CC   -!- SUBUNIT: Interacts with PBP1a. {ECO:0000255|HAMAP-Rule:MF_01890}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01890}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01890};
CC       Periplasmic side {ECO:0000255|HAMAP-Rule:MF_01890}.
CC   -!- SIMILARITY: Belongs to the LpoA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01890}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN82341.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN82341.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000249171.1; NC_004431.1.
DR   AlphaFoldDB; Q8FDA1; -.
DR   BMRB; Q8FDA1; -.
DR   SMR; Q8FDA1; -.
DR   STRING; 199310.c3900; -.
DR   EnsemblBacteria; AAN82341; AAN82341; c3900.
DR   KEGG; ecc:c3900; -.
DR   eggNOG; COG3107; Bacteria.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0031241; C:periplasmic side of cell outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cell outer membrane; Cell shape; Lipoprotein; Membrane; Palmitate;
KW   Peptidoglycan synthesis; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   CHAIN           27..678
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405932"
FT   REGION          304..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           27
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   LIPID           27
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ   SEQUENCE   678 AA;  72873 MW;  5A5D9CE21C290600 CRC64;
     MVPSTFSRLK AARCLPVVLA ALIFAGCGTH TPDQSTAYMQ GTAQADSAFY LQQMQQSSDD
     TRINWQLLAI RALVKEGKTG QAVELFNQLP QELNDTQRRE KTLLAAEIKL AQKDFAGAQN
     LLAKITPADL EQNQQARYWQ AKIDASQGRP SIDLLRALIA QEPLLGAKEK QQNIDATWQA
     LSSMTQEQAN TLVINADENI LQGWLDLQRV WFDNRNDPDM MKAGIADWQK RYPNNPGAKM
     LPTQLVNVKA FKPASTNKIA LLLPLNGQAA VFGRTIQQGF EAAKNIGTQP VVAQVAAAPA
     ADVAEQPQPQ TVDGVASPAQ ASVSDLTGEQ PAAQSVPVSA PATSTAAVSA PANPSAELKI
     YDTSSQPLSQ ILSQVQQDGA SIVVGPLLKN NVEELLKSNT PLNVLALNQP ENIENRVNIC
     YFALSPEDEA RDAARHIRDQ GKQAPLVLIP RSSLGDRVAN AFAQEWQKLG GGTVLQQKFG
     STSELRAGVN GGSGIALTGS PITPRETTDS GMTTNNPTLQ TTPTDDQFTN NGGRVDAVYI
     VATPGEIAFI KPMIAMRNGS QSGATLYASS RSAQGTAGPD FRLEMEGLQY SEIPMLAGGN
     LPLMQQALSA VNNDYSLARM YAMGVDAWSL ANHFSQMRQV QGFEINGNTG SLTANPDCVI
     NRKLSWLQYQ QGQVVPAS