ID   LPOA_SODGM              Reviewed;         670 AA.
AC   Q2NWH5;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-AUG-2022, entry version 74.
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=SG0226;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(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=BAE73500.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP008232; BAE73500.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2NWH5; -.
DR   SMR; Q2NWH5; -.
DR   STRING; 343509.SG0226; -.
DR   EnsemblBacteria; BAE73500; BAE73500; SG0226.
DR   KEGG; sgl:SG0226; -.
DR   eggNOG; COG3107; Bacteria.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   BioCyc; SGLO343509:SGP1_RS02065-MON; -.
DR   Proteomes; UP000001932; 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; 2.
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; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   CHAIN           27..670
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405945"
FT   REGION          258..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..338
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   670 AA;  70665 MW;  4395D1FA04AB89B6 CRC64;
     MLYSYVLVFK TGRLLPVVLA SLILAACTAQ GPESQTGHAA IPANANADYY LQQMQQSSND
     TKTDYQLLAI RALIKEGRLP QAQQQLAALQ QIDSASLDAP QRLRYTQAMI NAGQSRPSLD
     LVRAYIAQAP LLTDPAARQQ NIDKTWQTLV SLPSPQSNLV INADENILQG WLDLLRIYQD
     NRQDPTLLQA AIKDWQTRYP QNPAAKTLPT PLSQVQNYSS SSVGGIALLL PLNGQAQVFS
     NAIQQGFSAA KNGLTTQQSA LEQDASAAGQ STDGVPQNDG TAGTEPAGGS ANQNGPVTTP
     GTRPDPAASG VDGQASAADN APQATTLSGQ SAGGQPSAAP SAASGVPVKV YDTSSQPLPA
     LLAQAQRDGA SMIIGPLLKN DVEQLYNDNA VAASAGTLNI LALNQPEHLQ PRPNICYFAL
     SPEDEARDAA NHIHQQGRQQ PLLLLPRGAL GDRIAKAFSD AWHQAGGATV LEQRFGSSAE
     LKQNINSGSG ISLTGTPVAA GAAVTIAGLT IPVPQDNGAV SPSGGAIDAV YIIATPVELA
     LIKPMIDMRV SSRSRLALYA SSRSYQADAG PDYSLEMEGL EFSDIPLLTG AHPALLSQIS
     AQFRGDYSLV RLYAMGIDAW ALANHFSEMR QIPGFQVAGE TGTLSATPDC VINRTLSWLK
     YQRGQMIAAQ