BTUFA_HALS3
ID BTUFA_HALS3 Reviewed; 369 AA.
AC B0R5G2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Cobalamin-binding protein;
DE AltName: Full=Vitamin B12-binding protein;
DE Flags: Precursor;
GN Name=btuF; OrderedLocusNames=OE_2951R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
CC -!- FUNCTION: Required for corrinoid utilization. Probably part of the ABC
CC transporter complex BtuCDF involved in cobalamin (vitamin B12) import.
CC Probably binds cobalamin and delivers it to the surface of BtuC (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (BtuD),
CC two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).
CC {ECO:0000250}.
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; AM774415; CAP13979.1; -; Genomic_DNA.
DR RefSeq; WP_010902993.1; NC_010364.1.
DR AlphaFoldDB; B0R5G2; -.
DR SMR; B0R5G2; -.
DR EnsemblBacteria; CAP13979; CAP13979; OE_2951R.
DR GeneID; 5954317; -.
DR KEGG; hsl:OE_2951R; -.
DR HOGENOM; CLU_038034_2_1_2; -.
DR OMA; WQGINLE; -.
DR PhylomeDB; B0R5G2; -.
DR Proteomes; UP000001321; Chromosome.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR InterPro; IPR026469; Peripla_PGF_1.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR TIGRFAMs; TIGR04281; peripla_PGF_1; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
PE 3: Inferred from homology;
KW Signal; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..369
FT /note="Cobalamin-binding protein"
FT /id="PRO_0000408972"
FT DOMAIN 62..319
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT REGION 322..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 37713 MW; A0B96723BEB377C6 CRC64;
MHRGRFATLV IVALAVTMTA PAGALAPQPP AQHADADRAC SFPVTEPDAS NTAITLDSEP
ERVVTLNPSA AQTMWELGDR DAVVGVSQFG TYLPTASQRT VVSGGQPSQT NVEAVVGLDP
DLVLAPNTVR NTTVTRLRSA GITVFQFRAA TSIDGVVEKT ATIGRLTGNC AAAAATTAEM
RDRVAAIADA VPDTDSARPR VYYHLGDGYT AGPNTFIGAA IEAAGGHNIA ADVNTTSSYP
QLSEEVIVSQ DPDVVVTGVS ADRLDATASA LVAPSSVVRN TTAYATGNVV AVNTNHINQP
APRIVEPMAR MANAFHNTTI NTTLDAQPSA TTTATSTAPP TDAADGTAPG FGVAAAVCAL
AGAALVARR