LPOA_PHOPR
ID LPOA_PHOPR Reviewed; 613 AA.
AC Q6LME4;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=PBPRA3227;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378673; CAG21533.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6LME4; -.
DR SMR; Q6LME4; -.
DR STRING; 298386.PBPRA3227; -.
DR EnsemblBacteria; CAG21533; CAG21533; PBPRA3227.
DR KEGG; ppr:PBPRA3227; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_0_6; -.
DR OMA; MRLYAMG; -.
DR Proteomes; UP000000593; Chromosome 1.
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..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT CHAIN 30..613
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405941"
FT LIPID 30
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT LIPID 30
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ SEQUENCE 613 AA; 69215 MW; C23F5408E449F4D5 CRC64;
MNSMLNFTHK RKSVSRLLAP VALAVILAGC SSSNQQQASA SNITAIATDT SANYLIKAES
SDGIESIDWN ILALKALIKE GQWTQADNQS KRLSRMSLSP IQMAEWQLAR ATLRYQQGQL
QEALNTLNFQ PWWPLPDNQY KRYFMLRAEL LGQLGQHSKA ARQRTMLDQY LPSNQKNANW
QNLWQDLSSY NNSQLQSVSL KEDETVLRGW IQLSILKNTY SQRPVRLKSA VDEWLSMNPY
HPAHQYLPTE LEAIMSMEVA QLDNVALLLP LTGRFESQGK AVRDGFINAM LDDTSRDTDT
ELTVFDTEAE SMTAIMAKLQ ANGTQFVIGP LRKEKVTAFQ QSNTSQINLL ALNQPEQLDV
SQTQSCYFSL SPEQEAEQAA QHLFAKGHQY PLVLAPKSKF GQRMTDAFNE QWQQLTGRNA
DIDTFGSRKQ IQQQISRIFG LNDSQARISQ MNQLTGVKLE SQQRSRRDTD AVYLIANKSE
LTLLKPFIEV AINPEVKPPK LYASSRGNPN ANSDNSELRG IEFSDIPLII NPELSFMERF
DSLWPNESNT SIRLHAFGMD AYKMVNELPQ LRVVDNYTVQ GMTGQLGIDN QCVVQREMDW
AVFTSDGITP AAE
