LPOA_EDWTE
ID LPOA_EDWTE Reviewed; 692 AA.
AC D0ZBY2;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=ETAE_0536;
OS Edwardsiella tarda (strain EIB202).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=498217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EIB202;
RX PubMed=19865481; DOI=10.1371/journal.pone.0007646;
RA Wang Q., Yang M., Xiao J., Wu H., Wang X., Lv Y., Xu L., Zheng H., Wang S.,
RA Zhao G., Liu Q., Zhang Y.;
RT "Genome sequence of the versatile fish pathogen Edwardsiella tarda provides
RT insights into its adaptation to broad host ranges and intracellular
RT niches.";
RL PLoS ONE 4:E7646-E7646(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}.
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DR EMBL; CP001135; ACY83383.1; -; Genomic_DNA.
DR RefSeq; WP_012847407.1; NC_013508.1.
DR AlphaFoldDB; D0ZBY2; -.
DR SMR; D0ZBY2; -.
DR PRIDE; D0ZBY2; -.
DR EnsemblBacteria; ACY83383; ACY83383; ETAE_0536.
DR KEGG; etr:ETAE_0536; -.
DR HOGENOM; CLU_026091_1_1_6; -.
DR OMA; MRLYAMG; -.
DR OrthoDB; 776281at2; -.
DR Proteomes; UP000002634; 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..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT CHAIN 27..692
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405929"
FT REGION 297..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 692 AA; 72621 MW; DD7E648717BA45F8 CRC64;
MLSSITVRTK SGRLIPLVLA ATLLAACSGR VSTTPPAPVQ SEATASADYY LQQMQQSSDD
SKADWQLLAI RALLREGKLP QAADLLGQLP SQLSEAQQLE QRLVSAELEI ARHAPQQAQA
ILTKLDVAQL SQAQQLRYYQ AVIAAAQGKT TLAQIRAYIA LQPLLTQEKQ RKANIDATWA
ALSTLTPADL NGMVINANED ILRGWLDLLR LYQDNRQDPA LLKAAIKDWQ TRYPNNPAAT
LLPSALDNIL HLQSASTASI ALLLPLNGQA KVFSDAIEAG FNAAKNGAFS QNSAPTAAAA
TDNGAPASSG TLAAATTPSA PADVNAAGAV SPSAQGTDAA APAAPNDSAA LPPLDAAGDP
IAPSVSPGNP DAHIQVYDTS SQPLPALLSQ AQQAGASLVV GPLLKNNVDQ LNTLSTPLNI
LALNQPEQVQ NHPNICYFAL SPEDEARDAA RHIWAQGKRT PLLLIPRSPL GDRVAKAFAT
EWQSLGGGSV LQQTFGSSAE LRSTINGGTG IRLTGQPVSI APAQPASVTI AGLTIPAPVQ
PPVASGGGVD AVYIIATPAE ITLIKPMIDL ANGTHNGIGL YASSRSYQAG AGPDFRLEME
GVQFSDIPLL AGSDPAILQQ APAQYRNDYS LMRLYAMGAD AWTLANHFAQ LRQIPGFQVQ
GATGTLSAND NCVIQRKLPW LQYQKGSIVP VQ