ID   LPOA_SHIF8              Reviewed;         678 AA.
AC   Q0T0D4;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-AUG-2022, entry version 82.
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=SFV_3177;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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=ABF05231.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000266; ABF05231.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000249125.1; NC_008258.1.
DR   AlphaFoldDB; Q0T0D4; -.
DR   BMRB; Q0T0D4; -.
DR   SMR; Q0T0D4; -.
DR   EnsemblBacteria; ABF05231; ABF05231; SFV_3177.
DR   KEGG; sfv:SFV_3177; -.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   BioCyc; SFLE373384:SFV_RS17550-MON; -.
DR   Proteomes; UP000000659; 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_0000405942"
FT   REGION          300..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;  72725 MW;  7450002A6C69DEBD CRC64;
     MVPSTFSRLK AARCLPVVLA ALIFAGCGTH TPDQSTAYMQ GTAQADSAFY LQQMQQSSDD
     TRINWQLLAI RALVKEGKTG QAVELFNQLP QELNDSQRRE KTLLAAEIKL AQKDFAGAQN
     LLAKITPADL EQNQQARYWQ AKIDASQGRP SIDLLRALIA QEPLLGAKEK QQNIDATWQA
     LSSMTQEQAN TLVINADENI LQGWLDLQRV WFDNRNDPDM MKAGIADWQK RYPNNPGAKM
     LPTQLVNVKA FKPASTNKIA LLLPLNGQAA VFGRTIQQGF EAAKNIGTQP VAAQVAAAPA
     ADVAEQPQPQ TADGVASPAQ ASVSDLTGDQ PAAQPVPVSA PATSTAAVSA PANPSAELKI
     YDTSSQPLSQ ILSQVQQDGA SIVVGPLLKN NVEELLKSNT PLNVLALNQP ENIENRVNIC
     YFALSPEDEA RDAARHIRDQ GKQAPLVLIP RSALGDRVAN AFAQEWQKLG GGTVLQQKFG
     STSELRAGVN GGSGIALTGS PITPRATTDS GMTTNNPTLQ TTPTDDQFTN NGGRVDAVYI
     VATPGEIAFI KPMIAMRNGS QSGATLYASS RSAQGTAGPD FRLEMEGLQY SEIPMLAGGN
     LPLMQQALSA VNNDYSLARM YAMGVDAWSL ANHFSQMRQV QGFEINGNTG SLTANPDCVI
     NRKLSWLQYQ QGQVVPAS