LPQB_RHOJR
ID LPQB_RHOJR Reviewed; 597 AA.
AC Q0S2Y3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Lipoprotein LpqB {ECO:0000255|HAMAP-Rule:MF_01373};
DE Flags: Precursor;
GN Name=lpqB {ECO:0000255|HAMAP-Rule:MF_01373};
GN OrderedLocusNames=RHA1_ro06326;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01373};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01373}.
CC -!- SIMILARITY: Belongs to the LpqB lipoprotein family. {ECO:0000255|HAMAP-
CC Rule:MF_01373}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000431; ABG98103.1; -; Genomic_DNA.
DR RefSeq; WP_009479530.1; NC_008268.1.
DR AlphaFoldDB; Q0S2Y3; -.
DR SMR; Q0S2Y3; -.
DR STRING; 101510.RHA1_ro06326; -.
DR EnsemblBacteria; ABG98103; ABG98103; RHA1_ro06326.
DR KEGG; rha:RHA1_ro06326; -.
DR eggNOG; COG5401; Bacteria.
DR HOGENOM; CLU_032207_1_0_11; -.
DR OMA; CASMPDS; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR HAMAP; MF_01373; LpqB_lipoprot; 1.
DR InterPro; IPR019606; GerMN.
DR InterPro; IPR023959; Lipoprotein_LpqB.
DR InterPro; IPR018910; Lipoprotein_LpqB_C.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR Pfam; PF10646; Germane; 1.
DR Pfam; PF10647; Gmad1; 1.
DR SMART; SM00909; Germane; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01373"
FT CHAIN 29..597
FT /note="Lipoprotein LpqB"
FT /id="PRO_0000286728"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 29
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01373"
FT LIPID 29
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01373"
SQ SEQUENCE 597 AA; 62083 MW; EFAB8ECD0F3FC5BC CRC64;
MTPGRRSALL SRSVCGAIVL AVLVTVSGCA SLPDSSTPQA IGTINRDSPG SSVAAPAPGR
EPDLLLRDFF KASTDPSNRH LAARQFLTPG VSGRWDDAAS ATIVDKVDVL PETRSADQAT
YTIRANKVGQ LEPGGLYVAE EGSFETKISL ELQGGEWRIS ELPAGVILDR AQFLNTYQRK
SLYFLDPAGT TVVPDPRWVS GAQDQMASQL IGLLIDGPKA ALAPAVRNEL GDGVSVRGPI
TKADGRTAQV GVGLGGIRID FAGVPPMDAQ AKQLFAAQVI WTLANAEISG PYVLLADGEP
FDERFPNGWT TADVASMNPF ATSSATVGLH ALREGSMVSV TETGVTPVPG YFGSARNMRS
LALSQDGKLV AAVADTGRPA PEPASSLMVG AYEDGAASVL EGGAITRPTW APDNSAIWAA
VNGNTVIRVL REPGTGRTSV VNVDAGAVTA LGATITELRL SRDGVRAALI VDGKVYLAIV
TQMPGGEYAL TNPRAVAIGL GSPALSLDWS TSDTIVVARA ASDIPVVQVA VDGSRMDALP
SRNLTAPVVA VDASTTTEFV ADSRAVFQLN NNDPAGDRYW REVPGLTGVK AIPVLPG
