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Database: UniProt
Entry: A0A1B2M092_9GAMM
LinkDB: A0A1B2M092_9GAMM
Original site: A0A1B2M092_9GAMM 
ID   A0A1B2M092_9GAMM        Unreviewed;       266 AA.
AC   A0A1B2M092;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Biopolymer transport protein ExbB {ECO:0000256|ARBA:ARBA00022093};
GN   ORFNames=BFG52_09805 {ECO:0000313|EMBL:AOA58616.1};
OS   Acinetobacter larvae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1789224 {ECO:0000313|EMBL:AOA58616.1, ECO:0000313|Proteomes:UP000093391};
RN   [1] {ECO:0000313|EMBL:AOA58616.1, ECO:0000313|Proteomes:UP000093391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRTC-1 {ECO:0000313|EMBL:AOA58616.1,
RC   ECO:0000313|Proteomes:UP000093391};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the TonB-dependent energy-dependent transport of
CC       various receptor-bound substrates. Protects ExbD from proteolytic
CC       degradation and functionally stabilizes TonB.
CC       {ECO:0000256|ARBA:ARBA00024816}.
CC   -!- SUBUNIT: The accessory proteins ExbB and ExbD seem to form a complex
CC       with TonB. {ECO:0000256|ARBA:ARBA00011471}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004057}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU004057}.
CC   -!- SIMILARITY: Belongs to the exbB/tolQ family.
CC       {ECO:0000256|RuleBase:RU004057}.
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DR   EMBL; CP016895; AOA58616.1; -; Genomic_DNA.
DR   RefSeq; WP_067555391.1; NZ_CP016895.1.
DR   AlphaFoldDB; A0A1B2M092; -.
DR   STRING; 1789224.BFG52_09805; -.
DR   KEGG; ala:BFG52_09805; -.
DR   OrthoDB; 9805133at2; -.
DR   Proteomes; UP000093391; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002898; MotA_ExbB_proton_chnl.
DR   InterPro; IPR014164; TonB_ExbB_1.
DR   NCBIfam; TIGR02797; exbB; 1.
DR   PANTHER; PTHR30625:SF16; BIOPOLYMER TRANSPORT PROTEIN EXBB; 1.
DR   PANTHER; PTHR30625; PROTEIN TOLQ; 1.
DR   Pfam; PF01618; MotA_ExbB; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU004057};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093391};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU004057}.
FT   TRANSMEM        55..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          126..231
FT                   /note="MotA/TolQ/ExbB proton channel"
FT                   /evidence="ECO:0000259|Pfam:PF01618"
SQ   SEQUENCE   266 AA;  29198 MW;  BB546E9650A61443 CRC64;
     MKHPRSSLFR PFFKLLASFI VLLSFNSMCH AALPLSNISL SPLALFQQAD IVVKAVLIIL
     LLASFATWVA WLMKVLELKK QGRLVVRSML AIEQLNHLAD RIDLPNGATQ TMHHISAKEF
     QLAQSAGLQD ENTVKERVIS LTDRIISNEK HRLSHGTAIL ATTGAIAPFV GLFGTVWGIM
     HSFVAIAQSN VTNLSVVAPG IAEALFATAL GLFAAIPAVI FYNHVVRLIT QYGLLIEDTM
     ALLMVLLSRD LDQLAAQQRQ RPQGDD
//
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