ID   LPOA_SHIF2              Reviewed;         678 AA.
AC   D2A869;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   25-MAY-2022, entry version 58.
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=SFxv_3500;
OS   Shigella flexneri serotype X (strain 2002017).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002017;
RX   PubMed=19955273; DOI=10.1128/jcm.00614-09;
RA   Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA   Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA   Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT   "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT   clone of Shigella flexneri.";
RL   J. Clin. Microbiol. 48:419-426(2010).
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=ADA75514.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001383; ADA75514.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000249126.1; NC_017328.1.
DR   AlphaFoldDB; D2A869; -.
DR   BMRB; D2A869; -.
DR   SMR; D2A869; -.
DR   EnsemblBacteria; ADA75514; ADA75514; SFxv_3500.
DR   KEGG; sfe:SFxv_3500; -.
DR   PATRIC; fig|591020.3.peg.3771; -.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   Proteomes; UP000001884; 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_0000405943"
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        307..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;  72755 MW;  B99009EA6E85675A 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 TADSVASPAQ 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