ID A0A1G8MEK6_9RHOB Unreviewed; 231 AA.
AC A0A1G8MEK6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05421850_104161 {ECO:0000313|EMBL:SDI66413.1};
OS Lutimaribacter saemankumensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Lutimaribacter.
OX NCBI_TaxID=490829 {ECO:0000313|EMBL:SDI66413.1, ECO:0000313|Proteomes:UP000199340};
RN [1] {ECO:0000313|EMBL:SDI66413.1, ECO:0000313|Proteomes:UP000199340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28010 {ECO:0000313|EMBL:SDI66413.1,
RC ECO:0000313|Proteomes:UP000199340};
RA de Groot N.N.;
RL Submitted (OCT-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; FNEB01000004; SDI66413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8MEK6; -.
DR STRING; 490829.SAMN05421850_104161; -.
DR OrthoDB; 9805133at2; -.
DR Proteomes; UP000199340; 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:UP000199340};
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..46
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02202"
FT TRANSMEM 135..162
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02202"
FT TRANSMEM 182..200
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02202"
FT DOMAIN 112..215
FT /note="MotA/TolQ/ExbB proton channel"
FT /evidence="ECO:0000259|Pfam:PF01618"
SQ SEQUENCE 231 AA; 24986 MW; D4A24294C8949F88 CRC64;
MEAETLALAQ EMDFSMWSLF ARATLTVKLV MILLIVASFW SWSIIVQKLI AYRKARAEAA
VFDRAFWSGE PLDELFDQIG ADPAGRSERV FAAGMIEWRR SHRQDGGLIA GAQARIDRSM
DVAIAKEAED LQGGLSVLAT VGSVTPFVGL FGTVWGIMHA FIGIAEQQNT NLAVVAPGIA
EALLATGLGL LAAIPAVIFY NKLSADSDRI VAGYEAFADE FSTILSRQLD S
//
