ID   LPOA_MANSM              Reviewed;         574 AA.
AC   Q65T15;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=MS1288;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU37895.1; -; Genomic_DNA.
DR   RefSeq; WP_011200462.1; NC_006300.1.
DR   AlphaFoldDB; Q65T15; -.
DR   SMR; Q65T15; -.
DR   STRING; 221988.MS1288; -.
DR   EnsemblBacteria; AAU37895; AAU37895; MS1288.
DR   KEGG; msu:MS1288; -.
DR   eggNOG; COG3107; Bacteria.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   OMA; MRLYAMG; -.
DR   OrthoDB; 776281at2; -.
DR   Proteomes; UP000000607; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell shape; Lipoprotein; Membrane; Palmitate;
KW   Peptidoglycan synthesis; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   CHAIN           26..574
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405937"
FT   LIPID           26
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   LIPID           26
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ   SEQUENCE   574 AA;  63113 MW;  2C634FCDB7FD95EA CRC64;
     MTILLQRAKF KKRLMPILFP LMLAGCTNLF GSNFQDVLRN DANASSEFYM NKIEQTREVE
     DQQTYKLLAA RVLVTENKTA QAEALLAELT KLTPEQQLDK SILDALIAAV KRDNDSASAL
     LKTIPLAQLS QSQTSRYYEV QARIAENKTD IIEAVKARIQ MDMALTDVQR KQDNIDKIWA
     LLRSGNKTLI NTTQPEGNVA LAGWLDLTKA YNDNLSQPSQ LAQALQNWKT TYPNHSAAYL
     FPTELKSLSN FTQTQVNKIA LLLPLSGNAS ILGSTIKSGF DDSRGADKSV QVDVIDTMAM
     PVTDAIALAK QNGDGMIVGP LLKDNVDVIL SNPTAVQGMN VLALNSTPNA RAIDKMCYYG
     LAPEDEAEAA ANRMWNDGVR QPIVAVPQSD LGQRTASAFN VRWQQLAASD ADVRYYNQPD
     DAAYNLTADP AQNQAIYIVV TDSEQLMSIK GALDNSGVKA KIYTNSRNNS SNNAVEYRLA
     MEGVTFSDIP FFKDLDGEQY KKIEAATGGD YSLMRLYAMG ADSWLLAHSF NELRQVPGFS
     LSGLTGKLTA GPNCNVERDL TWYSYQGGNI VPLN