ID   LPOA_VIBCM              Reviewed;         603 AA.
AC   C3LS71;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   25-MAY-2022, entry version 52.
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=VCM66_0539;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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=ACP04864.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001233; ACP04864.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C3LS71; -.
DR   SMR; C3LS71; -.
DR   EnsemblBacteria; ACP04864; ACP04864; VCM66_0539.
DR   KEGG; vcm:VCM66_0539; -.
DR   HOGENOM; CLU_026091_1_0_6; -.
DR   Proteomes; UP000001217; Chromosome I.
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   Gene3D; 1.25.40.10; -; 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; PTHR38038; 1.
DR   Pfam; PF04348; LppC; 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..603
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405948"
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   603 AA;  67670 MW;  63A06E41877C200F CRC64;
     MAMNHHQRRS VPRLLTPIAL SIVLSACSTQ PSSPDVVDIT AQPLLTAQTY LMRADASQGN
     QQNDWLIMAL KAAIEENNPD QAQLLIMRLA KQPLTPTQQA QWQLLRAQLL ANTEQYQEAL
     EQLSFQANWS LPQVQWQQYH QLRADIFTAL DRSFDSTREL VALYGLSSNK DKEALADQIW
     ANLNHYSASK IIKLSTEPDE AQLDGWLQLA IYMKTLGSDL PQLKNTLEKW LAENPQHPAA
     IYTPKAITDI LALEIVKPTN TALLLPLTGK FAKQAQFIRD GFVFAMMNDA DRQTNATLTI
     IDTNAETLES VDAILTSKQI DFVVGPLIKG NIEKLQQFQQ SRGQMIPTLA LNIPDQIDTT
     AGACYLALSP EQEVAQAAKH LFTQGYRYPL ILAPQNAYGE RVVEAFNEEW RRYSKNKVAV
     NLFGDKRQLQ RNINSIFGLQ DSQQNIAQME SLLGMGLESQ PRSRRDIDAV YIVANSSELT
     LIKPFIEVAI NPDTRPPKLF SNSNSNTGGR QYEDLSGVTY SDIPLLIQPA PSIKEQLTQI
     WPESSNAERR LQALGMDAYR LMVELPQMKI VEGYTIDGQT GVLSIDEQCV VQREISWAEH
     GVR