ID   BION_RHOCB              Reviewed;         210 AA.
AC   D5ARG9;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Energy-coupling factor transporter transmembrane protein BioN;
DE            Short=ECF transporter T component BioN;
GN   Name=bioN; Synonyms=cbiQ3, ecfT; OrderedLocusNames=RCAP_rcc03250;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [2]
RP   EXPRESSION IN E.COLI, FUNCTION IN BIOTIN UPTAKE, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=17301237; DOI=10.1073/pnas.0609905104;
RA   Hebbeln P., Rodionov D.A., Alfandega A., Eitinger T.;
RT   "Biotin uptake in prokaryotes by solute transporters with an optional ATP-
RT   binding cassette-containing module.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2909-2914(2007).
RN   [3]
RP   SUBCELLULAR LOCATION, POSSIBLE TOPOLOGY, AND MUTAGENESIS OF ARG-164 AND
RP   ARG-195.
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=19717603; DOI=10.1128/jb.00965-09;
RA   Neubauer O., Alfandega A., Schoknecht J., Sternberg U., Pohlmann A.,
RA   Eitinger T.;
RT   "Two essential arginine residues in the T components of energy-coupling
RT   factor transporters.";
RL   J. Bacteriol. 191:6482-6488(2009).
CC   -!- FUNCTION: Probably involved in biotin uptake, although complementation
CC       experiments in E.coli do not indicate a clear role.
CC       {ECO:0000269|PubMed:17301237}.
CC   -!- SUBUNIT: Part of a biotin transporter holocomplex composed of BioM,
CC       BioN and BioY. BioMN complexes can be readily purified, but not BioNY
CC       complexes. Only the BioMNY complex has ATPase activity.
CC       {ECO:0000269|PubMed:17301237}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:17301237,
CC       ECO:0000305|PubMed:19717603}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:17301237, ECO:0000305|PubMed:19717603}.
CC   -!- SIMILARITY: Belongs to the CbiQ family. {ECO:0000305}.
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DR   EMBL; CP001312; ADE86974.1; -; Genomic_DNA.
DR   RefSeq; WP_013068947.1; NC_014034.1.
DR   AlphaFoldDB; D5ARG9; -.
DR   SMR; D5ARG9; -.
DR   STRING; 272942.RCAP_rcc03250; -.
DR   TCDB; 3.A.1.25.7; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; ADE86974; ADE86974; RCAP_rcc03250.
DR   GeneID; 31492031; -.
DR   KEGG; rcp:RCAP_rcc03250; -.
DR   eggNOG; COG0619; Bacteria.
DR   HOGENOM; CLU_056469_4_2_5; -.
DR   OMA; LWHGWTG; -.
DR   OrthoDB; 1479665at2; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR003339; ABC/ECF_trnsptr_transmembrane.
DR   Pfam; PF02361; CbiQ; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..210
FT                   /note="Energy-coupling factor transporter transmembrane
FT                   protein BioN"
FT                   /id="PRO_0000409020"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..33
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..98
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         164
FT                   /note="R->E: Approximately 3X reduction in BioMNY ATPase
FT                   activity. Loss of BioMNY complex assembly; when associated
FT                   with E-195."
FT                   /evidence="ECO:0000269|PubMed:19717603"
FT   MUTAGEN         195
FT                   /note="R->E: Approximately 3X reduction in BioMNY ATPase
FT                   activity. Loss of BioMNY complex assembly; when associated
FT                   with E-164."
FT                   /evidence="ECO:0000269|PubMed:19717603"
SQ   SEQUENCE   210 AA;  22327 MW;  1F3DF1DC63F7D896 CRC64;
     MLSLALPCRS WAHRLPAALK FGLLAVAMIA LMRIGSLAGQ GAAVLVVAAL TASLGRKAIR
     QSLVTLRPLV WIVAVILIWD SLQGAVAQGV LFGLRVLAMV GLANAVTLTT PLPEIVALIE
     RLAQPLARFG ISPRIPAISV ALVIRFVPVL RARHDTLAEA WRARSARKPR GKLLAPLTFS
     LLDDADHMAD ALRARGGLAL PRKGRDTVGT