ID   LPOA_KLEP7              Reviewed;         702 AA.
AC   A6TEG6;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   25-MAY-2022, entry version 64.
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=KPN78578_35260; ORFNames=KPN_03555;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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=ABR78950.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000647; ABR78950.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004185807.1; NC_009648.1.
DR   AlphaFoldDB; A6TEG6; -.
DR   SMR; A6TEG6; -.
DR   STRING; 272620.KPN_03555; -.
DR   EnsemblBacteria; ABR78950; ABR78950; KPN_03555.
DR   KEGG; kpn:KPN_03555; -.
DR   HOGENOM; CLU_026091_1_1_6; -.
DR   Proteomes; UP000000265; 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; 2.
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; Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT   CHAIN           27..702
FT                   /note="Penicillin-binding protein activator LpoA"
FT                   /id="PRO_0000405936"
FT   REGION          327..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..373
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   702 AA;  75084 MW;  CA2EEBC679DCCB6B CRC64;
     MVPSTFLRSK PARCLPVLLA TLIFAGCGTH TQDQSAAFMQ GTSQANSSFY LQQMQQSTND
     SKTNWQLLAI RALLQEGKKQ QAIDLFNQLP ANLNSTQARE QSLLAVEVKL AQNDYQAARN
     LLAKIDPTNL EQPQQARYWQ AQIDASQGKP SLTLLRALIA QQPLLSDAKQ RQKNIDATWQ
     ALTSMPQDQA NALVINADEN ILQGWLDLQR MWFDNRNDPT LLKAGVKDWQ TRYPQNPGAK
     MLPTALVNMQ NYKPASINKI ALFLPLNGQA SIFGRTIQQG FEAAKNGAPS VTGSAVPAQV
     AQAANVSGND DVVSPSQAEI SDLTATGSRA DPVQAPTQDQ AAPAAEPAAQ APATSTTPQT
     TASPATQPVT APAAQPQPVV ATAANPSAEL KIYDTTTQPI SQLLAQAQQD GATLVVGPLL
     KENVEEVIKS NTPLNVLALN QPEKVESRAN LCYFALSPED EARDAARHIH QQGKQTPLLL
     VPRGALGDRV VSAFADEWLK LGGASVLQQR FGSTAELRAG VNGGGGIALS GTPVSTLPSA
     QNSILGSADE MPVSSGGSVD AAYILATPEQ IAYIKPMIAM RNGSQSNVTL YASSRSAQGT
     AGPDFRLEME GLQYSEIPML AGSNPSLMQQ ALSAVRNDYS LARLYAMGAD AWSLANHFTQ
     MRQTPGFELN GNTGDLTANQ DCVINRKLSW LKYQQGKIVP AS