ID   LPOA_HAEDU              Reviewed;         583 AA.
AC   Q7VMZ8;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=HD_0803;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP95703.1; -; Genomic_DNA.
DR   RefSeq; WP_010944753.1; NC_002940.2.
DR   AlphaFoldDB; Q7VMZ8; -.
DR   SMR; Q7VMZ8; -.
DR   STRING; 233412.HD_0803; -.
DR   EnsemblBacteria; AAP95703; AAP95703; HD_0803.
DR   KEGG; hdu:HD_0803; -.
DR   eggNOG; COG3107; Bacteria.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   OMA; MRLYAMG; -.
DR   Proteomes; UP000001022; 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; 1.
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; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   CHAIN           25..583
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405933"
FT   LIPID           25
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   LIPID           25
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ   SEQUENCE   583 AA;  65072 MW;  71A92EAED1821E2B CRC64;
     MATILKQKLK TFFVPTAITL LLSACNSTSL FENSVTYLIK QEAYASSEFY INKAEQTLNS
     QDKITYQLLA VRKLIDENKV VEAQNTLNDL TTRLNIMEQN PLQQLEYQLV TAQLAALKGN
     NHQAEVTLQH ISAANLSHSQ LLRFYQTQAK IAENSKNTIE AVRIRSLIAT QLVDNKLRQE
     NNDKIWSLLR NANRGMLSSA QAGAGEMELA GWLALIEIYN QSVSTPAQMP QNINYWKRLY
     PNHSALAVMP TELQRVFNFQ QTLLNNVALL LPLSGDAKIL GEIIKKGFDD AKEQDPTIVQ
     VFDTDSNSIE NILMQAKQQG AQMIIGPLLK SRVNQMLASD QIRDINVLAL NATQDVKPIV
     GVCYYGLSPE AEARSGADRL SRDGYTKAIV VAARDEFGQR SAEAFAQRWR QLTNTDADIR
     YYNQPLDVIT TIQNSANNLQ ETALYALGNA EQLLEIKQGL ENSTIAGQLA IYTASRSNSP
     NNGIEFRTAM EGVKFSEIPL LADHNSNEYQ KAYSLADSDF SMMRLYAMGS DTWALANKFN
     EFRQIPGYSI SGLTGNLNAG PNCNIERNMT WLQYHNGAVE TTN