LPQB_MYCTO
ID LPQB_MYCTO Reviewed; 587 AA.
AC P9WK36; L0TC87; O05889; Q7D5U9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Lipoprotein LpqB {ECO:0000255|HAMAP-Rule:MF_01373};
DE Flags: Precursor;
GN Name=lpqB {ECO:0000255|HAMAP-Rule:MF_01373}; OrderedLocusNames=MT3342;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: May modulate activity of the MtrAB system in controlling
CC homeostasis of the cell wall and cell division. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MtrB, probably extracytoplasmically.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01373};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01373}. Secreted, cell wall
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LpqB lipoprotein family. {ECO:0000255|HAMAP-
CC Rule:MF_01373}.
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DR EMBL; AE000516; AAK47684.1; -; Genomic_DNA.
DR PIR; F70592; F70592.
DR AlphaFoldDB; P9WK36; -.
DR SMR; P9WK36; -.
DR EnsemblBacteria; AAK47684; AAK47684; MT3342.
DR KEGG; mtc:MT3342; -.
DR HOGENOM; CLU_032207_1_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 Pfam; PF10646; Germane; 1.
DR Pfam; PF10647; Gmad1; 1.
DR SMART; SM00909; Germane; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall; Lipoprotein; Membrane; Palmitate; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01373"
FT CHAIN 20..587
FT /note="Lipoprotein LpqB"
FT /id="PRO_0000427722"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01373"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01373"
SQ SEQUENCE 587 AA; 61681 MW; 1E2C7D25A2C5D91B CRC64;
MERLMRLTIL LFLGAVLAGC ASVPSTSAPQ AIGTVERPVP SNLPKPSPGM DPDVLLREFL
KATADPANRH LAARQFLTES ASNAWDDAGS ALLIDHVVFV ETRSAEKVSV TMRADILGSL
SDVGVFETAE GQLPDPGPIE LVKTSDGWRI DRLPNGVFLD WQQFQETYKR NTLYFADPTG
KTVVPDPRYV AVSDRDQLAT ELVSKLLAGP RPEMARTVRN LLAPPLRLRG PVTRADGGKS
GIGRGYGGAR VDMEKLSTTD PHSRQLLAAQ IIWTLARADI RGPYVINADG APLEDRFAEG
WTTSDVAATD PGVADGAAAG LHALVNGSLV AMDAQRVTPV PGAFGRMPEQ TAAAVSRSGR
QVASVVTLGR GAPDEAASLW VGDLGGEAVQ SADGHSLSRP SWSLDDAVWV VVDTNVVLRA
IQDPASGQPA RIPVDSTAVA SRFPGAINDL QLSRDGTRAA MVIGGQVILA GVEQTQAGQF
ALTYPRRLGF GLGSSVVSLS WRTGDDIVVT RTDAAHPVSY VNLDGVNSDA PSRGLQTPLT
AIAANPSTVY VAGPQGVLMY SASVESRPGW ADVPGLMVPG AAPVLPG