ID   LPOA_ENT38              Reviewed;         721 AA.
AC   A4WEW2;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   24-JAN-2024, entry version 88.
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=Ent638_3584;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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=ABP62242.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000653; ABP62242.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041689536.1; NC_009436.1.
DR   AlphaFoldDB; A4WEW2; -.
DR   SMR; A4WEW2; -.
DR   STRING; 399742.Ent638_3584; -.
DR   KEGG; ent:Ent638_3584; -.
DR   eggNOG; COG3107; Bacteria.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   OrthoDB; 6708821at2; -.
DR   Proteomes; UP000000230; Chromosome.
DR   GO; GO:0031241; C:periplasmic side of cell outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd06339; PBP1_YraM_LppC_lipoprotein-like; 1.
DR   Gene3D; 1.25.40.650; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   HAMAP; MF_01890; LpoA; 1.
DR   InterPro; IPR007443; LpoA.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR38038; PENICILLIN-BINDING PROTEIN ACTIVATOR LPOA; 1.
DR   PANTHER; PTHR38038:SF1; PENICILLIN-BINDING PROTEIN ACTIVATOR LPOA; 1.
DR   Pfam; PF04348; LppC; 2.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 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..721
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405930"
FT   REGION          316..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..393
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   721 AA;  76589 MW;  27E37115684B6662 CRC64;
     MVPLTFLRTK ASRSLPIMLA ALIFAGCGTQ APDQTAAHMQ GSAQADSGFY LQQMSQSSND
     TKTNWQLLAI RALLNEGKTQ QAVDLYNQLP QELNNTQRGE QSLLAAELKI AQKEYPAAKK
     LLADIDTKAL ENNQQARYWQ AVIAAEQGRP SLPLLRALIA QEPLLSGADK QKNIDTTWQA
     LSSMTPEQSQ ALVINADENV LQGWLDLQQM WFNNRSDPKM LKAGITDWQT RYPQNPGAKM
     LPTQLVNVQN FQPASVSKIA LLLPLNGQAA VFGRTIQQGF EAAKNGTTAV AGNAVPAQAA
     QAANVNDVIS PSAVETSDLT SAQAPAQGTM QNPVTAPTTP PATTQAPAET AAPAEAQTPV
     VPQAAPATDA ATAQPQTTTP DQQPAAQPQA VAATTANPGA ELKIYDTSSQ PLDQVLAQVQ
     KDGASIVVGP LLKNNVEELM KSNTSLNVLA LNQPEQVQNR ANICYFALSP EDEARDAARH
     IHEQGKQAPL LLTPRSALGD RVATAFAQEW QQLGGNIVLQ QKFGSTSELR AGVNGGSGIA
     LTGSPVSASL PQQQGVTIGG LTIPAPPTDA QISGGGKVDA AYIVATPEEI AFIKPMIAMR
     NGSQSGVTLY ASSRSAQGTA GPDFRLEMDG LQYSEIPMLA GSNPALMQQA LSSVRNDYSL
     ARLYAMGVDA WALANHFTQM RQVPGFELNG NTGDLTATQD CVINRKLSWL KYQQGQIVPA
     S
//