LPOA_EDWI9
ID LPOA_EDWI9 Reviewed; 682 AA.
AC C5B768;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 25-MAY-2022, entry version 66.
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=NT01EI_0614;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR67842.2; -; Genomic_DNA.
DR RefSeq; WP_015870039.1; NC_012779.2.
DR AlphaFoldDB; C5B768; -.
DR SMR; C5B768; -.
DR STRING; 67780.B6E78_13765; -.
DR EnsemblBacteria; ACR67842; ACR67842; NT01EI_0614.
DR GeneID; 7960381; -.
DR KEGG; eic:NT01EI_0614; -.
DR PATRIC; fig|634503.3.peg.557; -.
DR HOGENOM; CLU_026091_1_1_6; -.
DR OrthoDB; 776281at2; -.
DR Proteomes; UP000001485; 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; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT CHAIN 27..682
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405928"
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 682 AA; 72557 MW; 5ADD63E814B96EBC CRC64;
MLSSITVRTK SGRLIPLVLA ATLLAACSGR ISTTPPAPVQ SEATASADYY LQQMQQSSDD
SKADWQLLAI RALLREGKLP QADDLLGQLP SQLTEAQQLE QRLVSAELEI ARHAPQQAQA
ILSKLDISLL SQAQQLRYYQ AVIAAVQGKT TLAQIRAYIA LQPLLTQENQ RKSNIDATWT
ALNTLTPADL NSMVINANED ILRGWLDLLR LYQDNRQDPA LLKAAIKEWQ TRYPNNPAAT
MLPSALDNIL HLQSDSTASI ALLLPLNGQA KVFSDAIEAG FNAAKNGAFN QNSAAVTTDG
TPTAQVDAPA QPDVNAAGAV STSTQSADAT ASVLPADSAA LPPLDAAGDP IAPSVSPGNP
DAHIQVYDTS SQPLPELLSQ AQQAGVSLVI GPLLKNNVDQ LNTISTPLNI LALNQPEQVQ
NHPNICYFAL SPEDEARDAA RHIWAQGKRT PLLLIPRNPL GDRVAKAFAT EWQSLGGGSV
LRQTFGSSAE LRSTINSGTG IRLTGQPVSI TPAQPTSVTI AGLTIPAPVQ PPVASGGGVD
AVYIIATPAE ITLIKPMIDL ANGTHNGISL YASSRSYQAG AGPDFRLEME GVQFSDIPLL
AGSDPAILQQ APAQYRNDYS LMRLYAMGAD AWTLANHFAQ LRQIPGFQVQ GATGTLSASD
NCVIQRKLPW LQYQKGSIVP VL