LPOB_YERE8
ID LPOB_YERE8 Reviewed; 193 AA.
AC A1JME2;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Penicillin-binding protein activator LpoB {ECO:0000255|HAMAP-Rule:MF_01889};
DE Short=PBP activator LpoB {ECO:0000255|HAMAP-Rule:MF_01889};
DE Flags: Precursor;
GN Name=lpoB {ECO:0000255|HAMAP-Rule:MF_01889}; OrderedLocusNames=YE1703;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential for
CC the function of penicillin-binding protein 1B (PBP1b).
CC {ECO:0000255|HAMAP-Rule:MF_01889}.
CC -!- SUBUNIT: Interacts with PBP1b. {ECO:0000255|HAMAP-Rule:MF_01889}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01889}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01889};
CC Periplasmic side {ECO:0000255|HAMAP-Rule:MF_01889}.
CC -!- SIMILARITY: Belongs to the LpoB family. {ECO:0000255|HAMAP-
CC Rule:MF_01889}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAL11778.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AM286415; CAL11778.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_042661400.1; NC_008800.1.
DR RefSeq; YP_001005989.1; NC_008800.1.
DR AlphaFoldDB; A1JME2; -.
DR SMR; A1JME2; -.
DR STRING; 393305.YE1703; -.
DR EnsemblBacteria; CAL11778; CAL11778; YE1703.
DR KEGG; yen:YE1703; -.
DR PATRIC; fig|393305.7.peg.1846; -.
DR eggNOG; COG3417; Bacteria.
DR HOGENOM; CLU_092328_0_0_6; -.
DR Proteomes; UP000000642; 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 HAMAP; MF_01889; LpoB; 1.
DR InterPro; IPR014094; LpoB.
DR InterPro; IPR012640; Membr_lipoprot_lipid_attach_CS.
DR PANTHER; PTHR40593; PTHR40593; 1.
DR Pfam; PF08139; LPAM_1; 1.
DR Pfam; PF13036; LpoB; 1.
DR TIGRFAMs; TIGR02722; lp; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cell shape; Lipoprotein; Membrane; Palmitate;
KW Peptidoglycan synthesis; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT CHAIN 17..193
FT /note="Penicillin-binding protein activator LpoB"
FT /id="PRO_0000405794"
FT REGION 24..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 17
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
FT LIPID 17
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01889"
SQ SEQUENCE 193 AA; 20520 MW; 8254F6E0CE8509DC CRC64;
MKRYLSVALA ALVLTGCITQ PPVEPTTPPV TIEPVTPPVP ETPPPVDNVP PPPKMEQSID
WAASVEPLVA QMVNSNDVAN GSILLLDSVK NNTNGRLPTA KATSALHQVL SSNKKFVLIS
PQQLAVAKQT LGLSEEDSLG SRSKAIGLAR YVSAQYVLYS DVSGDVKSPT IEMQLMQAQT
GEIIWSGNGP VKR