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LPOA_VIBAE
ID   LPOA_VIBAE              Reviewed;         603 AA.
AC   D0M814;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   25-MAY-2022, entry version 51.
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}; OrderedLocusNames=VEA_004501;
OS   Vibrio antiquarius (strain Ex25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio diabolicus subgroup.
OX   NCBI_TaxID=150340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ex25;
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA   Bartels D.;
RT   "Sequence of the deep-sea isolate Vibrio sp. strain Ex25.";
RL   Submitted (OCT-2009) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACY52659.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001805; ACY52659.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_006743240.1; NZ_DS267860.1.
DR   AlphaFoldDB; D0M814; -.
DR   SMR; D0M814; -.
DR   KEGG; vex:VEA_004501; -.
DR   OrthoDB; 776281at2; -.
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; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   CHAIN           25..603
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405951"
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   603 AA;  67673 MW;  1D71EBF52AA557F9 CRC64;
     MINHKRLSVP RILTPVALAI TLAACSSGPR QPDGVDVTLE PTQSVQNYMI QADSTEGSLR
     NDWLIMATKA AIQANQFDQA ELLIKRLARQ QLTEVQQAEW QLARATIQQK QGNYSQLLQL
     LNFKPWWKLP NEQWKDYYLM RADAYQGLNQ AFEANRQLVA FGQYASSAEQ REISSRIWMN
     FGSYSEYELT SLETEPNEDV LDGWLQLAVY AKTLSGNLSQ LKNTLERWLS ENPSHPAAIY
     TPEEIQNILS LDIVKPNNTA LLLPLTGKFS PQAQLIRDGF VFAMMNDRNR DPSATLTVID
     TNAYNADQIK QRLINKNIDF VVGPLEKENV ELLHTTMDGS ANGPTIPALA LNIPEDVQPD
     SNICYLALSP EQEAAQAAKH LFSEGYNFPL ILAPKGSFGE RVTEAFNKEW RKYSSNKVAA
     SYFGDKRQLQ KDINEVFGLQ ESKQRIAQMQ SLMRIKLETQ PRSRRDVDAV YIVARSTELT
     LIKPFIEVAI NPDAKAPQIF SSSRSNSGGA TYEDLTGIIY SDIPLLIDPD PSVTAEMNEL
     WSEQSNMEKR LKALGMDAYK LIGELPQMKV VPGYSVGGQT GILSIDNNCV VQRELSWAER
     GAL
 
 
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