(data stored in ACNUC7421 zone)

SWISSPROT: 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   07-JUN-2017, entry version 38.
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=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
CC       for 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}.
DR   EMBL; CP001600; ACR67842.2; -; Genomic_DNA.
DR   RefSeq; WP_015870039.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0614; -.
DR   EnsemblBacteria; ACR67842; ACR67842; NT01EI_0614.
DR   GeneID; 7960381; -.
DR   KEGG; eic:NT01EI_0614; -.
DR   PATRIC; fig|634503.3.peg.557; -.
DR   eggNOG; ENOG4105E1C; Bacteria.
DR   eggNOG; COG3107; LUCA.
DR   HOGENOM; HOG000125217; -.
DR   KO; K07121; -.
DR   OrthoDB; POG091H068H; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_01890; LpoA; 1.
DR   InterPro; IPR007443; LpoA.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   Pfam; PF04348; LppC; 2.
DR   SUPFAM; SSF53822; SSF53822; 3.
PE   3: Inferred from homology;
DR   PRODOM; C5B768.
DR   SWISS-2DPAGE; C5B768.
KW   Cell outer membrane; Cell shape; Complete proteome; Lipoprotein;
KW   Membrane; Palmitate; Peptidoglycan synthesis; Reference proteome;
KW   Signal.
FT   SIGNAL        1     26       {ECO:0000255|HAMAP-Rule:MF_01890}.
FT   CHAIN        27    682       Penicillin-binding protein activator
FT                                LpoA.
FT                                /FTId=PRO_0000405928.
FT   LIPID        27     27       N-palmitoyl cysteine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01890}.
FT   LIPID        27     27       S-diacylglycerol cysteine.
FT                                {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
//

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