LPOA_ERWT9
ID LPOA_ERWT9 Reviewed; 670 AA.
AC B2VDC8;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
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}; OrderedLocusNames=ETA_29200;
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
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}.
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DR EMBL; CU468135; CAO97966.1; -; Genomic_DNA.
DR RefSeq; WP_012442620.1; NC_010694.1.
DR AlphaFoldDB; B2VDC8; -.
DR SMR; B2VDC8; -.
DR STRING; 465817.ETA_29200; -.
DR EnsemblBacteria; CAO97966; CAO97966; ETA_29200.
DR KEGG; eta:ETA_29200; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_1_6; -.
DR OMA; MRLYAMG; -.
DR OrthoDB; 776281at2; -.
DR Proteomes; UP000001726; 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..670
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405931"
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; 71852 MW; AA1AF70C6A988158 CRC64;
MLPSKVVHRK AVRTVPLLLA ALIFAGCTGQ APHTPPANVQ GAADGTSDYY LQQVQQSADD
NKVDWQLLAI RALLNEGKLP QAGDALTQLP ADLNNIQRQE RLLLLARLNV ARQNLSGATD
PLKQIDISAL SQQQQVRYYQ LQIAVGQGQP SLDVVRAWVA LEPLQTSPAD KQKNIDETWQ
ALLQIPQQQI NTLTINANEN VLQGWLDLLG VYKNNVTAPD MLKSAIQDWQ TRYPYNPAAK
MLPTSLTQAQ NLHPASMGKI ALLLPLSGQA QVFANAIQKG FNDAKNGVLA QSTVAPSPAG
PVQVPAATPG DAAVAVSPSA TTSDKAVAEQ PAPAINVTTA APSASTQIQV YDTSSQPVEQ
LLTQAQNDGA TLAIGPLLKS DVDKMLNSQT ALNVLALNEP ESVQNRPNIC YFALSPEDEA
RDAAHHMWEQ GKRAPLLLVP RTSLGDRVNK AFAAEWQKLG GATVLQQQFG STAELKQGIN
SGAGIRLSGT PVNVQPQQQA GVTIAGLTIP APPTDAQPGA TSSNGRVDSV YIVATQDEMI
LIKPMIAMRI SSRDNVGLYA SSRSYQAGAG PDYRLELEGL QFSDAPLLSG ANPALMQQAA
KAFNNDYSLV RLYAMGVDAW TLANHFNEMR NQPGFQIKGD TGMLSANQDC IINRKLVWSQ
YHQGQIVPGT