BIOM_RHOCB
ID BIOM_RHOCB Reviewed; 234 AA.
AC D5ARH0;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Biotin transport ATP-binding protein BioM;
DE EC=7.6.2.-;
DE AltName: Full=ECF transporter A component BioM;
GN Name=bioM; OrderedLocusNames=RCAP_rcc03251;
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, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-41.
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).
CC -!- FUNCTION: Required for biotin uptake under very low (pM) biotin
CC concentrations but not under higher (nM) concentrations.
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 BioMY
CC complexes. Only the BioMNY complex has ATPase activity.
CC {ECO:0000269|PubMed:17301237}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:17301237}; Peripheral membrane protein
CC {ECO:0000305|PubMed:17301237}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; CP001312; ADE86975.1; -; Genomic_DNA.
DR RefSeq; WP_013068948.1; NC_014034.1.
DR AlphaFoldDB; D5ARH0; -.
DR SMR; D5ARH0; -.
DR STRING; 272942.RCAP_rcc03251; -.
DR TCDB; 3.A.1.25.7; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE86975; ADE86975; RCAP_rcc03251.
DR GeneID; 31492032; -.
DR KEGG; rcp:RCAP_rcc03251; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_1_22_5; -.
DR OMA; MSILAME; -.
DR OrthoDB; 1713578at2; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..234
FT /note="Biotin transport ATP-binding protein BioM"
FT /id="PRO_0000409019"
FT DOMAIN 1..230
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 41
FT /note="K->N: Diminished biotin uptake, loss of ATPase
FT activity, BioMNY complexes still form."
FT /evidence="ECO:0000269|PubMed:17301237"
SQ SEQUENCE 234 AA; 25114 MW; 84FCE533FCC4541E CRC64;
MQAIDIGHVT LERDGTGVFS DLTLRLTERR IGIVGRNGAG KSSLIRLITG LVTPQKGRVV
VNGVDVAADR AGALGTVGLL FQNPDHQIIF PVVRDEIAFG LEQKGLKRAA ALARAEAVLA
AQGRADWGDR LCHTLSQGQR QLLCLMSILA MEPDWILFDE PFNALDLPTA LSIEARIAGL
AQNVVLVTHD PSRLTGFDRI LWLEGGRIEA DGPPAEVLPR YIAAMQALAR AGAC