ID   LPOA_SHISS              Reviewed;         678 AA.
AC   Q3YX94;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=SSON_3293;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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; CP000038; AAZ89868.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3YX94; -.
DR   BMRB; Q3YX94; -.
DR   SMR; Q3YX94; -.
DR   EnsemblBacteria; AAZ89868; AAZ89868; SSON_3293.
DR   KEGG; ssn:SSON_3293; -.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   OMA; MRLYAMG; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0031241; C:periplasmic side of cell outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; IPR008939; Lytic_TGlycosylase_superhlx_U.
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; SSF48435; SSF48435; 1.
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..678
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405944"
FT   REGION          302..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..329
FT                   /note="Polar residues"
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   678 AA;  72869 MW;  3E8E267CABF5C755 CRC64;
     MVPSTFSRLK AARCLPVVLA ALIFAGCGTH TPDQSTAYMQ GTAQADSAFY LQQMQQSSDD
     TRINWQLLAI RALVKEGKTG QAVELFNQLP QELNDSQRRE KTLLAVEIKL AQKDFAGAQN
     LLAKITPADL EQNQQARYWQ AKIDASQGRP SIDLLRALIA QEPLLGAKEK KQNIDATWQA
     LSSMTQEQAN TLVINADENI LQGWLDLQRV WFDNRNDPDM MKAGIADWQK RYPNNPGAKM
     LPTQLVNVKA FKPASTNKIA LLLPLNGQAA VFGRTIQQGF EAAKNIGTQP VAAQVAAAPA
     ADVAEQPQPQ TVDGVASPAQ ASVSDLTGDQ PAAQPVPVSA PATSTAAVSA PANPSAELKI
     YDTSSQPLSQ ILSQVQQDGA SIVVGPLLKN NVEELLKSNT PLNVLALNQP ENIENRVNIC
     YFALSPEDEA RDAARHIRDQ GKQAPLVLIP RSSLGDRVAN AFAQEWQKLG GGTVLQQKFG
     STSELRAGVN GGSGIALTGT PITPRATTDS GMTTNNPTLQ TTPTDDQFTN NGGRVDAVYI
     VATPGEIAFI KPMIAMRNGS QSGAMLYASS RSAQGTAGPD FRLEMEGLQY SEIPMLAGGN
     LPLMQQALSA VNNDYSLARM YAMGVDAWSL ANHFSQMRQV QGFEINGNTG SLTANPDCVI
     NRKLSWLQYQ QGQVVPVS