LPOA_YERP3
ID LPOA_YERP3 Reviewed; 657 AA.
AC A7FDZ0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 25-MAY-2022, entry version 65.
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};
GN OrderedLocusNames=YpsIP31758_0475;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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=ABS49021.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000720; ABS49021.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012303495.1; NC_009708.1.
DR AlphaFoldDB; A7FDZ0; -.
DR SMR; A7FDZ0; -.
DR EnsemblBacteria; ABS49021; ABS49021; YpsIP31758_0475.
DR KEGG; ypi:YpsIP31758_0475; -.
DR HOGENOM; CLU_026091_1_1_6; -.
DR Proteomes; UP000002412; Chromosome.
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; 2.
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..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT CHAIN 26..657
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405954"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ SEQUENCE 657 AA; 70216 MW; 6AF96F352B8941C1 CRC64;
MLSSTFVRSK AGLVPVILAA LILAACTGDA PQTPPPVNIQ DEASANSDYY LQQLQQSSDD
NKADWQLLAI RALLREAKVP QAAEQLSTLP ANLSDTQRQE QQLLAAELLI AQKNTPAAAD
ILAKLEATQL SANQKVRYYQ AQIAANQDKA TLPLIRAFIA QEPLLTDKAH QDNIDGTWQS
LSQLTPQELN TMVINADENV LQGWLDLLRV YQDNKQDPEL LKAGIKDWQT RYPQNPAAKN
LPTALTQISN FSQASTAKIA LLLPLSGPAQ VFADAIQQGF TAAQNGSAVT ASVPVTPNVT
ESSPTDTAAV VSDDTPATLP APVTPPVVTN AQVKIYDTNT QPLAALLAQA QQDGATLVVG
PLLKPEVEQL SATPSTLNIL ALNQPEASNN SPNICYFALS PEDEARDAAH HLWEQQKRMP
LLLVPRGALG ERIAKAFADE WQKQGGQTVL QQNFGSTTEL KQSINSGAGI RLTGTPVSVS
NVAAAPASVT IAGLTIPAPP IDAPVVSTSS SGNIDAVYII ATPSELTLIK PMIDMATSSR
SKPALFASSR SYQAGAGPDY RLEMEGIQFS DIPLMAGSNP ALLQQASAKY ANDYSLVRLY
AMGIDAWALA NHFSEMRQIP GFQVKGVTGD LTASSDCVIT RKLPWLQYRQ GMVVPLA