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Database: UniProt
Entry: A0A1T5C333_9GAMM
LinkDB: A0A1T5C333_9GAMM
Original site: A0A1T5C333_9GAMM 
ID   A0A1T5C333_9GAMM        Unreviewed;       255 AA.
AC   A0A1T5C333;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Biopolymer transport protein ExbB {ECO:0000256|ARBA:ARBA00022093};
GN   ORFNames=SAMN05660880_01490 {ECO:0000313|EMBL:SKB53739.1};
OS   Luteibacter sp. 22Crub2.1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1283288 {ECO:0000313|EMBL:SKB53739.1, ECO:0000313|Proteomes:UP000191150};
RN   [1] {ECO:0000313|EMBL:SKB53739.1, ECO:0000313|Proteomes:UP000191150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22Crub2.1 {ECO:0000313|EMBL:SKB53739.1,
RC   ECO:0000313|Proteomes:UP000191150};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUYT01000006; SKB53739.1; -; Genomic_DNA.
DR   RefSeq; WP_036109039.1; NZ_FUYT01000006.1.
DR   AlphaFoldDB; A0A1T5C333; -.
DR   Proteomes; UP000191150; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002898; MotA_ExbB_proton_chnl.
DR   PANTHER; PTHR30625:SF14; BIOPOLYMER TRANSPORT PROTEIN EXBB; 1.
DR   PANTHER; PTHR30625; PROTEIN TOLQ; 1.
DR   Pfam; PF01618; MotA_ExbB; 1.
PE   3: Inferred from homology;
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   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        36..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          122..227
FT                   /note="MotA/TolQ/ExbB proton channel"
FT                   /evidence="ECO:0000259|Pfam:PF01618"
SQ   SEQUENCE   255 AA;  27601 MW;  7182DBEFEE89852D CRC64;
     MLQDTSAQPA QPGQNSNADA LKQMGFDHLI HNFDPLGWIV FVVLVAMSVL SWYFIVANFI
     RNSMVRARAD KVIQGFWNTS STQEAIRMLE EQPKGEPFSK IALDAASAVA HHQQAAGGRL
     AETLSRSEFI DRALRQAVAR ESLRLEGGLT LLATVGSSAP FIGLLGTVWG IYHALIGIAA
     SGSASMDKVA GPVGEALIMT AFGLFTAIPA VLAYNFFMRS NRLTYAKFDE FAHDLHDFFA
     TGARVEGTAP VVVKK
//
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