ID   LPOA_VIBVY              Reviewed;         603 AA.
AC   Q7MNW1;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Penicillin-binding protein activator LpoA;
DE            Short=PBP activator LpoA;
DE   Flags: Precursor;
GN   Name=lpoA; OrderedLocusNames=VV0604;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential for
CC       the function of penicillin-binding protein 1A (PBP1a). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PBP1a. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LpoA family. {ECO:0000305}.
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DR   EMBL; BA000037; BAC93368.1; -; Genomic_DNA.
DR   RefSeq; WP_011149497.1; NC_005139.1.
DR   AlphaFoldDB; Q7MNW1; -.
DR   SMR; Q7MNW1; -.
DR   STRING; 672.VV93_v1c05460; -.
DR   EnsemblBacteria; BAC93368; BAC93368; BAC93368.
DR   KEGG; vvy:VV0604; -.
DR   PATRIC; fig|196600.6.peg.623; -.
DR   eggNOG; COG3107; Bacteria.
DR   HOGENOM; CLU_026091_1_0_6; -.
DR   OMA; MRLYAMG; -.
DR   OrthoDB; 776281at2; -.
DR   Proteomes; UP000002675; 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   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|PROSITE-ProRule:PRU00303"
FT   CHAIN           25..603
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405952"
FT   LIPID           25
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           25
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   603 AA;  67832 MW;  B0B61A768DE74B03 CRC64;
     MMNPKRLSVP RLLTPVALAI TLAACSSGPK TPTSVDITLE PTLSVQNYMI NADSSEGSLQ
     ADWLIMAAKA ALQNGDLAQA DLLIKRLARM PLSEVQQAEW QLTRAAYHLK LNQADNVIEL
     LNFKAWWKLP NEQWKDYYTL RVEAYTALQQ PFEANRQLVT LSQYVDESQQ AEIAQQIWAN
     FTGYSQYEIT QLHPDASEEV LDGWLQLAIY MKTMSANVPQ LKNTLEHWFA ENTAHPAALY
     TPAEIQSILD LEIVQPVHTA LLLPLSGKYA KQAQLIRDGF IFAMMNDKDR DPEATLKVID
     TNLYQPHQLK QQLTDEQIDF IVGPLRKDVI EVLQGELSDD SGQVSIPSLA LNIPDELQTG
     TGICYLTLSP EQEVAQAAKH LFANGYKYPL IFAPQGNLGQ RVVSAFEAEW KKYSTNKVAV
     SYFGDKRQLQ RDVNSVFGLQ ESQQRIAQME GLMKLPMETQ PRSRRDIDSV YIAARSSELT
     LIKPFIEVAV NPDAKPPKLF SNSMSNSGEK QYEDLTGIVY SDIPMLLEVN PALDSQMEQL
     WPDQSNFQKR LQALGMDAYK LMAELPQMKV VPNHAVNGQT GVLTIDDQCV VHREISWKEH
     GAL