BTUB_ENT38
ID BTUB_ENT38 Reviewed; 615 AA.
AC A4WG45;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Vitamin B12 transporter BtuB {ECO:0000255|HAMAP-Rule:MF_01531};
DE AltName: Full=Cobalamin receptor {ECO:0000255|HAMAP-Rule:MF_01531};
DE AltName: Full=Outer membrane cobalamin translocator {ECO:0000255|HAMAP-Rule:MF_01531};
DE Flags: Precursor;
GN Name=btuB {ECO:0000255|HAMAP-Rule:MF_01531}; OrderedLocusNames=Ent638_4020;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
CC -!- FUNCTION: Involved in the active translocation of vitamin B12
CC (cyanocobalamin) across the outer membrane to the periplasmic space. It
CC derives its energy for transport by interacting with the trans-
CC periplasmic membrane protein TonB. {ECO:0000255|HAMAP-Rule:MF_01531}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01531}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01531}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. BtuB (TC
CC 1.B.14.3.1) subfamily. {ECO:0000255|HAMAP-Rule:MF_01531}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABP62675.1; Type=Erroneous initiation; Evidence={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; CP000653; ABP62675.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015960979.1; NC_009436.1.
DR AlphaFoldDB; A4WG45; -.
DR SMR; A4WG45; -.
DR STRING; 399742.Ent638_4020; -.
DR EnsemblBacteria; ABP62675; ABP62675; Ent638_4020.
DR KEGG; ent:Ent638_4020; -.
DR eggNOG; COG4206; Bacteria.
DR HOGENOM; CLU_008287_18_5_6; -.
DR OMA; SYELQWR; -.
DR OrthoDB; 71288at2; -.
DR Proteomes; UP000000230; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR HAMAP; MF_01531; BtuB; 1.
DR InterPro; IPR010101; B12_transptr_BtuB.
DR InterPro; IPR039426; BtuB-like.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR010916; TonB_box_CS.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR010917; TonB_rcpt_CS.
DR PANTHER; PTHR30069; PTHR30069; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR TIGRFAMs; TIGR01779; TonB-B12; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1.
PE 3: Inferred from homology;
KW Calcium; Cell outer membrane; Ion transport; Membrane; Metal-binding;
KW Porin; Signal; TonB box; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT CHAIN 21..615
FT /note="Vitamin B12 transporter BtuB"
FT /id="PRO_0000316877"
FT TRANSMEM 157..164
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 168..177
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 183..194
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 216..226
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 231..247
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 264..278
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 280..297
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 310..326
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 329..338
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 354..370
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 372..382
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 386..401
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 404..418
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 435..444
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 450..459
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 474..491
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 495..510
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 518..530
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 536..551
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 559..573
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 586..597
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 603..615
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT MOTIF 25..32
FT /note="TonB box"
FT MOTIF 598..615
FT /note="TonB C-terminal box"
FT BINDING 84
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 91
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 109..110
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 250
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 310
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 518
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
SQ SEQUENCE 615 AA; 68143 MW; AB63939938311FF0 CRC64;
MIKKVSLMTA LSVTAFSGWA QDSADSLVVT ANRFEQPANT VLAPTSVVTR EDIERWQSTT
VLDVMRRLPG VDTAQNGGMG QASSLFVRGT NSSHVLILVD GIRLNQAGVT GSSDLSQFPI
SLVQRIEYIR GPRSAVYGSD AIGGVVNIIT TRAKDGTTLN AGVGSHGYQN YGGSTQQTLG
DNTRVTLAGD YTYTKGFDVV ADGNNGGLAQ TDRDGYMNKT IYGALEHAFS DQWSGFVRGF
GYSNRTAYDA YYSSFTPDVL VDTRQLYSQT WDTGLRFNDG IFHSQLLSSY SHSKDYNYDP
HLGRYDSTAT LDEIKQYNVQ WTNSVDVGHG NVGAGVDWQK QSTEPGTNYV TNDTNLRNTG
VYLTALQKFG DFTLEGAARS DDNSQFGRHG TWQSSAAWEF IEGYRFIASY GTAYKAPNLG
QLYGFYGNDH LNPEESKQWE GAFEGLTAGV SWRVSAYRND VDNLIDFDSN LQQYYNVGKA
RIKGVEATAS FDTGPLTHTV GYDYVDARNA ATNELLDRRA KQQVKYQLDT QVYDFDWSLT
YHYLGTRYDT DFGSYPYQKV KMGGVSLWDL AVSYPVTSHL TVRGKIANLF DKDYETVYGY
ETAGREYTLS GSYTF
