ID A0A1M7D2X4_9GAMM Unreviewed; 228 AA.
AC A0A1M7D2X4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Tol-Pal system protein TolQ {ECO:0000256|HAMAP-Rule:MF_02202};
GN Name=tolQ {ECO:0000256|HAMAP-Rule:MF_02202};
GN ORFNames=SAMN05428972_0965 {ECO:0000313|EMBL:SHL73743.1};
OS Rhodanobacter sp. OK091.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1881037 {ECO:0000313|EMBL:SHL73743.1, ECO:0000313|Proteomes:UP000184078};
RN [1] {ECO:0000313|EMBL:SHL73743.1, ECO:0000313|Proteomes:UP000184078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK091 {ECO:0000313|EMBL:SHL73743.1,
RC ECO:0000313|Proteomes:UP000184078};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the Tol-Pal system, which plays a role in outer
CC membrane invagination during cell division and is important for
CC maintaining outer membrane integrity. {ECO:0000256|HAMAP-
CC Rule:MF_02202}.
CC -!- SUBUNIT: The Tol-Pal system is composed of five core proteins: the
CC inner membrane proteins TolA, TolQ and TolR, the periplasmic protein
CC TolB and the outer membrane protein Pal. They form a network linking
CC the inner and outer membranes and the peptidoglycan layer.
CC {ECO:0000256|HAMAP-Rule:MF_02202}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02202}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02202}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ExbB/TolQ family.
CC {ECO:0000256|ARBA:ARBA00010442, ECO:0000256|HAMAP-Rule:MF_02202}.
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DR EMBL; FRCH01000001; SHL73743.1; -; Genomic_DNA.
DR RefSeq; WP_072758342.1; NZ_FRCH01000001.1.
DR AlphaFoldDB; A0A1M7D2X4; -.
DR STRING; 1881037.SAMN05428972_0965; -.
DR OrthoDB; 9805133at2; -.
DR Proteomes; UP000184078; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043213; P:bacteriocin transport; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02202; TolQ; 1.
DR InterPro; IPR002898; MotA_ExbB_proton_chnl.
DR InterPro; IPR014163; Tol-Pal_TolQ.
DR NCBIfam; TIGR02796; tolQ; 1.
DR PANTHER; PTHR30625; PROTEIN TOLQ; 1.
DR PANTHER; PTHR30625:SF3; TOL-PAL SYSTEM PROTEIN TOLQ; 1.
DR Pfam; PF01618; MotA_ExbB; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02202};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02202};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_02202};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02202};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02202};
KW Reference proteome {ECO:0000313|Proteomes:UP000184078};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02202};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02202}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02202"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02202"
FT TRANSMEM 171..193
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02202"
FT DOMAIN 82..208
FT /note="MotA/TolQ/ExbB proton channel"
FT /evidence="ECO:0000259|Pfam:PF01618"
SQ SEQUENCE 228 AA; 25371 MW; 6A9057A0E2BF99BB CRC64;
MNGGLNIFSL IADSSLPVQL VLLVLLVFSF LSWVIIIRKY TQTKAAMEDA EAFEERFWSG
GDLAQLFREV SGRGADNGGI ENIFESGFRE FARQRQRKTH DVRSVMESSE RAMQVTGTRE
IGLLERNLEF LANVGSISPY VGLFGTVWGI MGAFQGLGEM KDVTIAVVAP HISEALIATA
MGLFAAIPAQ WAYNRYATKV ERIASRYDVF QEEFSSVLQR QIQTDDVA
//
