ID   LPOA_PASMU              Reviewed;         571 AA.
AC   Q9CN03;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 94.
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}; Synonyms=lppC;
GN   OrderedLocusNames=PM0646;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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DR   EMBL; AE004439; AAK02730.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9CN03; -.
DR   SMR; Q9CN03; -.
DR   STRING; 747.DR93_1476; -.
DR   EnsemblBacteria; AAK02730; AAK02730; PM0646.
DR   KEGG; pmu:PM0646; -.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   OMA; MRLYAMG; -.
DR   Proteomes; UP000000809; 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   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; 2.
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; Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   CHAIN           27..571
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405939"
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   571 AA;  63325 MW;  35AECE474784301F CRC64;
     MMTILLQHTH LKNRLMPFLL ALFLAGCTTF LGGGSASLLQ SDANANSDFY MNKVYQAQNL
     EEQHTYKLLA ARVLVTENKI PQAQALLNEL TTLTDEQVLD KSIIEAHIAA VKQQNTVADT
     QLKHINLAQL SRSQLARYYD VAARIAENRY DAIEAVKARI QIDQLLSDVS RKQANIDRTW
     SLLRNANRGV INNTVAEGNI ALGGWLALTR AYNQNLSNPA QLSQAIQQWK TAYPTHPAAY
     LFPTELQGLF NFQQTQFSQV ALLLPLSGNA QVIGNTIKAG FDAAKDNSAT QVQVFDTAAT
     PVDVIFDQVK QAGIRTVVGP LLKQNVDMLL NNAQLVQGLD VLTLNSTSNE RAIGQLCYYG
     LSPEDEAESA ANKMWKDGIR TPSVFVPQND LGRRTASAFN VRWQQLAATD ANIRFYNLPA
     DITYTLDDQN TSGVYIVAMS DQLAEIKTTI DNSGRTTKLY ASSRSNSANN APEYRLLMEG
     LQFSDIPFFK DVTSNQYKKI EKLTKGDFSL MRLYAMGADA WLLINHFNEL RQVPGYNIDG
     LTGKLSAGAN CNIERDMTWF QYQSGGIISL N