LPOA_VIBCJ
ID LPOA_VIBCJ Reviewed; 603 AA.
AC C3NVZ3;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 25-MAY-2022, entry version 50.
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=VCD_001027;
OS Vibrio cholerae serotype O1 (strain MJ-1236).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=593588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ-1236;
RX PubMed=19720995; DOI=10.1073/pnas.0907787106;
RA Chun J., Grim C.J., Hasan N.A., Lee J.H., Choi S.Y., Haley B.J.,
RA Taviani E., Jeon Y.-S., Kim D.W., Lee J.-H., Brettin T.S., Bruce D.C.,
RA Challacombe J.F., Detter J.C., Han C.S., Munk A.C., Chertkov O.,
RA Meincke L., Saunders E., Walters R.A., Huq A., Nair G.B., Colwell R.R.;
RT "Comparative genomics reveals mechanism for short-term and long-term clonal
RT transitions in pandemic Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15442-15447(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACQ59210.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001485; ACQ59210.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; C3NVZ3; -.
DR SMR; C3NVZ3; -.
DR KEGG; vcj:VCD_001027; -.
DR HOGENOM; CLU_026091_1_0_6; -.
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; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT CHAIN 27..603
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405949"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ SEQUENCE 603 AA; 67670 MW; 63A06E41877C200F CRC64;
MAMNHHQRRS VPRLLTPIAL SIVLSACSTQ PSSPDVVDIT AQPLLTAQTY LMRADASQGN
QQNDWLIMAL KAAIEENNPD QAQLLIMRLA KQPLTPTQQA QWQLLRAQLL ANTEQYQEAL
EQLSFQANWS LPQVQWQQYH QLRADIFTAL DRSFDSTREL VALYGLSSNK DKEALADQIW
ANLNHYSASK IIKLSTEPDE AQLDGWLQLA IYMKTLGSDL PQLKNTLEKW LAENPQHPAA
IYTPKAITDI LALEIVKPTN TALLLPLTGK FAKQAQFIRD GFVFAMMNDA DRQTNATLTI
IDTNAETLES VDAILTSKQI DFVVGPLIKG NIEKLQQFQQ SRGQMIPTLA LNIPDQIDTT
AGACYLALSP EQEVAQAAKH LFTQGYRYPL ILAPQNAYGE RVVEAFNEEW RRYSKNKVAV
NLFGDKRQLQ RNINSIFGLQ DSQQNIAQME SLLGMGLESQ PRSRRDIDAV YIVANSSELT
LIKPFIEVAI NPDTRPPKLF SNSNSNTGGR QYEDLSGVTY SDIPLLIQPA PSIKEQLTQI
WPESSNAERR LQALGMDAYR LMVELPQMKI VEGYTIDGQT GVLSIDEQCV VQREISWAEH
GVR