LPOA_PANAM
ID LPOA_PANAM Reviewed; 677 AA.
AC D4GNT6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 53.
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=PANA_3474;
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103;
RX PubMed=20348253; DOI=10.1128/jb.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(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=ADD78641.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001875; ADD78641.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041457821.1; NC_013956.2.
DR AlphaFoldDB; D4GNT6; -.
DR SMR; D4GNT6; -.
DR STRING; 706191.PANA_3474; -.
DR EnsemblBacteria; ADD78641; ADD78641; PANA_3474.
DR KEGG; pam:PANA_3474; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_1_6; -.
DR OMA; MRLYAMG; -.
DR OrthoDB; 776281at2; -.
DR BioCyc; PANA706191:PANA_RS17630-MON; -.
DR Proteomes; UP000001702; 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; 1.
DR Pfam; PF04348; LppC; 2.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..677
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405938"
FT REGION 309..359
FT /note="Disordered"
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 677 AA; 72482 MW; 1982C362A64A74E4 CRC64;
MLPSKIVRHK AGRFVPVLLA GLILAACSGQ GPKSQSVDIQ APVTNNSAYY LQQVQQSSDD
SKTDWQLLAI RALLKEGKYP QAAQAIGELP NQLSDKQQQE LLLLKAQSLV AQQKIADAQP
ILSQVKTSEL SQDQLARYYG LQIASAQGKT SLALLRAYIA QEPLLKGDER QQNIDATWQA
LTQLSQQDMN SLVINADENI LQGWLDLLTA WHANAQDANM LKSAIKDWQT RYPDNPAAKT
LPTQLSQVQN FTKASTSTIA LLLPLNGQAQ MFASAIQKGF NDAKNGTLAT APQATPGSAQ
DPIAINQQQP ADANAVVSPS ANPAAAQQSG TAQQPATTQQ QPQQQPAAEP ASNAQVKVYD
TSSQPIAQVM QQAQQDGATL VVGPLLKNNV ETVANSQTPL NVLALNEPEQ IQNHPNMCYF
ALSPEDEARD AAHHIWDQGK RQPLLLVPRN GLGDRVTAAF TKEWQSLGGG TVLQQRFGSV
SELKQGINSG AGISMSGTPV VMPSSSQPQS VSVAGLNIPA PQTSAPAASS GGAIDAAYIV
STQDELQLIK PMISMRTGSR SNVALYASSR SAQAGAGPDF RLEMEGLQFS DIPLLSGANP
ALMQQAAKSF NNDYSLVRLY AMGIDAWTLS NHFNQMRQVP GFSLDGNTGK LSATADCVIN
RKLTWNQYRQ GNIVPAS