BTUB_PECAS
ID BTUB_PECAS Reviewed; 615 AA.
AC Q6CZB5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=ECA4238;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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}.
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DR EMBL; BX950851; CAG77135.1; -; Genomic_DNA.
DR RefSeq; WP_011095709.1; NC_004547.2.
DR AlphaFoldDB; Q6CZB5; -.
DR SMR; Q6CZB5; -.
DR STRING; 218491.ECA4238; -.
DR EnsemblBacteria; CAG77135; CAG77135; ECA4238.
DR GeneID; 57210910; -.
DR KEGG; eca:ECA4238; -.
DR PATRIC; fig|218491.5.peg.4315; -.
DR eggNOG; COG4206; Bacteria.
DR HOGENOM; CLU_008287_18_5_6; -.
DR OMA; SYELQWR; -.
DR OrthoDB; 71288at2; -.
DR Proteomes; UP000007966; 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; 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; PS01156; TONB_DEPENDENT_REC_2; 1.
PE 3: Inferred from homology;
KW Calcium; Cell outer membrane; Ion transport; Membrane; Metal-binding;
KW Porin; Reference proteome; Signal; TonB box; Transmembrane;
KW Transmembrane beta strand; 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_0000003483"
FT TRANSMEM 158..165
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 169..178
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 184..195
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 257..271
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 273..290
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 303..319
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 322..331
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 347..363
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 365..375
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 379..394
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 397..411
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 429..438
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 444..453
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 468..486
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 490..505
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 513..525
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 531..546
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 26..33
FT /note="TonB box"
FT MOTIF 598..615
FT /note="TonB C-terminal box"
FT BINDING 85
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 92
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 110..111
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 199
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 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 303
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 513
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 547
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
SQ SEQUENCE 615 AA; 67860 MW; 49512456EA9C19F5 CRC64;
MIKKISLLTA LSVTAFSGWA QETDNNAMVV TANRFQQPVN SVLAPTTVVT REEIDRWQAK
SLTDVMRRLP GVDIGQNGGL GQKSSLFIRG TNSSHVLVLI DGIRLNQAGI SGSSDLSQIP
LSLVQKVEYI RGSRSAVYGS DAIGGVVNII TTREKNGTTL NAGVGSKGYQ SYDAATQQAL
GDSTTATLAG NYVYTKGFDV VAYGTASPAQ PDRDGFMSKS LYGTVEHKFG DQFSGFLRGY
GYDNRTDYDN FSSVDTRQLY SQTWDTGLRY QSGIYSTQLI GSYSHSKDYD YDPLRGLHSS
GSTLVDSQQY NAQWGNVLQV GAGTVSAGVD WQDQIIKPDS TSVNREESQN NTGIYLTGQQ
RFASIVLEGS VRGDDQSEFG WHNTWRTGAS WEFIEGYSLI ASYGTAFKAP NMGQLYGRFG
SNRDLQPEES KQWESGVEGL TGPVIWRVSG YRNDIDNLID ATGSTGYVYE NVGKAKIKGI
EATASFDTGP VGHRISYDYV DSRNAITDEP LARRAKQQVK YQLDWQVYDL DWSVTYQYLG
SRYDKDYGNY IPAVDDYQTV KLGGVSLWDL AASYPVTSHL TVRGRIANLF DKDYETAYGY
RTAGREYYLT GSYTF
