LPOA_ALIF1
ID LPOA_ALIF1 Reviewed; 603 AA.
AC Q5E2P0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=VF_2211;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(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; CP000020; AAW86706.1; -; Genomic_DNA.
DR RefSeq; WP_011262640.1; NC_006840.2.
DR RefSeq; YP_205594.1; NC_006840.2.
DR AlphaFoldDB; Q5E2P0; -.
DR SMR; Q5E2P0; -.
DR STRING; 312309.VF_2211; -.
DR EnsemblBacteria; AAW86706; AAW86706; VF_2211.
DR KEGG; vfi:VF_2211; -.
DR PATRIC; fig|312309.11.peg.2250; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_0_6; -.
DR OMA; MRLYAMG; -.
DR OrthoDB; 776281at2; -.
DR Proteomes; UP000000537; 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 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; Reference proteome; 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_0000405950"
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; 67947 MW; BEE1AC929ADAD949 CRC64;
MANMTPRKNS VTRLIAPVAL ALTLAACSSS PKAPDRLDIT QSPTETSNAY ILKADQQQGA
LEADFLIMAL KAAVQEQNFD LADKLFTRLA TMQLSPAQTA EMQLAHAKML KSQSQYEDAL
KTLNFEAWWK LENSQWVEYH KLRHELYLLS GDNLNSAREL IELEPFTAED QKAQLWTQVW
TSVSSLNSTA LEEVKLDETE TNLHGWVQLA TYLDTLKHSP MRLQETLNEW LLANPTHPAA
TYTPQVILDI LALEIVRPEN VALLLPLSGR FGPQGIRVRD GFINAMMEDK ERDEFTKLKV
IDTQATSMAE IMTTLEKEQI QFVVGPLVRS KIEEFQSLNS TEIAQLALNI PSEIDTDINS
CYFTLSPEQE AEQAAVHLFK QGFKHPLYLA PQGTMGERLS QAFSDKWFQL TAKRPSISYF
GSKAQLQQKV NSVFGIESSQ ARIYQMNALA SMELEAQPRS RRDIDAVYMV AKSSELVLLK
PFIEVAINPG IKPPKLYASS RSNSGRQTQL VEIKGIEFSD IPLLTNENHS FKAQYDELWP
KSSNGETRLH ALGMDAYQLV AELPQMKAVD NYRMEGKTGE LSLNQECVIQ RKMSWAVHGE
ETE