ID   BEXB1_HAEIF             Reviewed;         265 AA.
AC   P19390;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Capsule polysaccharide export inner-membrane protein BexB;
GN   Name=bexB;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RM 153 / Serotype B;
RX   PubMed=2137816; DOI=10.1128/jb.172.3.1374-1379.1990;
RA   Kroll J.S., Moxon E.R.;
RT   "Capsulation in distantly related strains of Haemophilus influenzae type b:
RT   genetic drift and gene transfer at the capsulation locus.";
RL   J. Bacteriol. 172:1374-1379(1990).
CC   -!- FUNCTION: May form an ATP-driven capsule polysaccharide export
CC       apparatus, in association with the BexA, BexC and BexD proteins.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M33787; AAA24945.1; -; Genomic_DNA.
DR   RefSeq; WP_015702019.1; NZ_VOFX01000001.1.
DR   AlphaFoldDB; P19390; -.
DR   SMR; P19390; -.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR000412; ABC_2_transport.
DR   Pfam; PF01061; ABC2_membrane; 1.
DR   PRINTS; PR00164; ABC2TRNSPORT.
DR   PROSITE; PS51012; ABC_TM2; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Cell inner membrane; Cell membrane;
KW   Membrane; Polysaccharide transport; Sugar transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..265
FT                   /note="Capsule polysaccharide export inner-membrane protein
FT                   BexB"
FT                   /id="PRO_0000182976"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..258
FT                   /note="ABC transmembrane type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ   SEQUENCE   265 AA;  30181 MW;  0A436FF824CD25C1 CRC64;
     MQYGDKTTFK QSLAIQGRVI NALLMREIIT RYGRQNIGFF WLFVEPLLMT FFIVMMWKFI
     RADKFSTLNM IAFVMTGYPM AMMWRNASNR AIGSISANLS LLYHRNVRVL DTIFTRVLLE
     VAGASIAQIL FMAILVMIDW IDAPHDVFYM LIAWFLMAMF AFGLGLIICA IAQQFDVFGK
     IWGTLSFVLL PISGAFFFVH NLPAQAQSIA LWFPMIHGTE MFRHGYFGDT VVTYESIGFL
     VVSDLALLLL GLVMVKNFSK GVEPQ