ID   LPOA_GLAP5              Reviewed;         578 AA.
AC   B8F4Z1;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=HAPS_0749;
OS   Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/jb.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(2009).
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; CP001321; ACL32393.1; -; Genomic_DNA.
DR   RefSeq; WP_012621890.1; NC_011852.1.
DR   AlphaFoldDB; B8F4Z1; -.
DR   SMR; B8F4Z1; -.
DR   STRING; 557723.HAPS_0749; -.
DR   EnsemblBacteria; ACL32393; ACL32393; HAPS_0749.
DR   KEGG; hap:HAPS_0749; -.
DR   PATRIC; fig|557723.8.peg.748; -.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   OMA; MRLYAMG; -.
DR   Proteomes; UP000006743; 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.
PE   3: Inferred from homology;
KW   Cell outer membrane; Cell shape; Lipoprotein; Membrane; Palmitate;
KW   Peptidoglycan synthesis; Reference proteome; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   CHAIN           31..578
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405934"
FT   LIPID           31
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   LIPID           31
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ   SEQUENCE   578 AA;  63995 MW;  17252FB81CBAA763 CRC64;
     MPTILVQSYG FRQKMKTIFI PTALALLLAA CSGNKVTETL KNEAYGNSEF YINKAEQSRN
     IEEQQSYRLL AVRKLIEENK VVEAQNTFSE ILVAKLNDEQ KLEHRLLIAQ LAALQGNTEA
     QGVLRALPQT LLSQSQRLRV YQTQARIAEN QNDVIAAVNA RALMDSYMTD TQSRQANNDK
     IWEMLRNANR GMLEKAVAGP GEIGLAGWLA LVVAYNQNMS NPAQLPQVIE MWKQQYPNHS
     AVLLLPIELR NVSSFQQTQL NGVALLLPLS GDAKILGEII KRGFDDAKGT TTMQVQVFDT
     DSAPINDLLM QAKQQGAQTI IGPLLKPRVD EMLTSPEISN INVLALNSTP NVRAVAKVCY
     YGLSPEAEAR SAAERFLKDG LQHAVVVAPN GDFGTRSAEA FAQRWRQLTN RDTDIRYYNQ
     AFEVTSLLQG SGIGQGSGLY ALGTAEQLSD LKQSLDNSPL ANQFPIYTSS RSNSPNNGPD
     FRLTMEGVKF SEIPLLSDPS SSEYKKAEQI VESDFSMMRL YAMGSDTWSI ANKFNEFRQI
     PGYKVHGLTG VLSAGPNCNI EREMNWLQYR GGSIVDAN