ID   LPOB_YERP1              Reviewed;         191 AA.
AC   D0JWX6;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   25-MAY-2022, entry version 47.
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=YPD8_2117;
OS   Yersinia pestis (strain D182038).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=637385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D182038;
RX   PubMed=19815893; DOI=10.4269/ajtmh.2009.09-0174;
RA   Zhang Z., Hai R., Song Z., Xia L., Liang Y., Cai H., Liang Y., Shen X.,
RA   Zhang E., Xu J., Yu D., Yu X.J.;
RT   "Spatial variation of Yersinia pestis from Yunnan Province of China.";
RL   Am. J. Trop. Med. Hyg. 81:714-717(2009).
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=ACY62794.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001589; ACY62794.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002213089.1; NC_017160.1.
DR   AlphaFoldDB; D0JWX6; -.
DR   SMR; D0JWX6; -.
DR   KEGG; ypx:YPD8_2117; -.
DR   PATRIC; fig|637385.3.peg.2810; -.
DR   HOGENOM; CLU_092328_0_0_6; -.
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..191
FT                   /note="Penicillin-binding protein activator LpoB"
FT                   /id="PRO_0000405796"
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   191 AA;  20223 MW;  883FC58F58BA1B72 CRC64;
     MKRYLSLALA ALVLTGCVPP DSVTPTPPVT IEPVTPPDVE VPPPVDTVPQ PPKVQSIDWA
     VSVEPLVAQM VNSDEVATGS ILLVDSVKNN TNGALQTAKA TAALHQVLSS NKKFVLISPQ
     QLGVAKQTLG LSEEDSFGSR SKAIGLARYV GAQYVLYSDV SGDVKSPTIE MQLMQTQTGE
     IIWSGNAPVQ Y