ID   A0A212QT37_9PROT        Unreviewed;       239 AA.
AC   A0A212QT37;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=SAMN07250955_103179 {ECO:0000313|EMBL:SNB62760.1};
OS   Arboricoccus pini.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Arboricoccus.
OX   NCBI_TaxID=1963835 {ECO:0000313|EMBL:SNB62760.1, ECO:0000313|Proteomes:UP000197065};
RN   [1] {ECO:0000313|EMBL:SNB62760.1, ECO:0000313|Proteomes:UP000197065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B29T1 {ECO:0000313|EMBL:SNB62760.1,
RC   ECO:0000313|Proteomes:UP000197065};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FYEH01000003; SNB62760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212QT37; -.
DR   OrthoDB; 9805133at2; -.
DR   Proteomes; UP000197065; 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:UP000197065};
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        28..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02202"
FT   TRANSMEM        139..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02202"
FT   TRANSMEM        182..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02202"
FT   DOMAIN          112..218
FT                   /note="MotA/TolQ/ExbB proton channel"
FT                   /evidence="ECO:0000259|Pfam:PF01618"
SQ   SEQUENCE   239 AA;  26051 MW;  BB6310E52C0FA0C9 CRC64;
     MEQSAVTTAG LASVATPSIL HLILEADLIV KAVMILLLCA SLWCWAVVFE KGFRFARLQR
     LATAFERNFW SGAPLDDLYR RLGKRPDHPM ALMFATAMDE WRESPSSSET AAQASLLERV
     GRVMSLTMDR EVQSLEKHLP SLATIGAVAP FVGLFGTVWG IMNSFQSIAA TKNTTLAVVA
     PGIAEALFAT AMGLVAAIPA VVAYNKLSYA LDRYAERLSS FTDEFSVVVS RELDAKRFG
//