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BTUB_CITFR
ID   BTUB_CITFR              Reviewed;         612 AA.
AC   O52903;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 103.
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};
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8090 / DSM 30039 / JCM 1657 / LMG 3246 / NCTC 9750;
RA   Letley D.P., Ward R.J., Glass R.E.;
RT   "Cloning and chimeric analysis of Citrobacter freundii BtuB defines
RT   residues essential for phage BF23 infection.";
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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; Y09059; CAA70262.1; -; Genomic_DNA.
DR   PIR; S77723; S77723.
DR   AlphaFoldDB; O52903; -.
DR   SMR; O52903; -.
DR   STRING; 1333848.CFNIH1_07425; -.
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..612
FT                   /note="Vitamin B12 transporter BtuB"
FT                   /id="PRO_0000003478"
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        217..227
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        232..248
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        263..277
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        279..296
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        309..325
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        328..337
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        353..369
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        371..381
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        385..400
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        403..417
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        434..443
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        449..458
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        473..490
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        494..509
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        517..529
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        535..550
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        556..570
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        583..594
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   TRANSMEM        600..612
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   MOTIF           26..33
FT                   /note="TonB box"
FT   MOTIF           595..612
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         211
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         215
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         215
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="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         250
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         250
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         261
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         309
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         517
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   BINDING         551
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
SQ   SEQUENCE   612 AA;  68125 MW;  1040A58DC318D63E CRC64;
     MIKKSLLCTA LSVTAFSGWA QDTRPDTLVV TANRFQQPRS AVLAPITVVT RQDIDRWQST
     SVNDVLRRLP GVDIAQYGGM GQNSSISIRG TNASHVLVLI DGVRLNLAGV SGAADLSQFP
     VSLVQRIEYI RGPRSAVYGS DAIGGVVNII TTREKPGTEL TAGVGSNGYQ NYDVSTQQQL
     GENTRVTLMG DYAYTKGFDV VAYGSTGSQA QPDKDGFLSK TLYGALEHNF SDTWSGFVRG
     YGYDNRTNYD SYYSPGSPLL DTRKLYSQSW DAGLRFNGEL IQSQLVSSYS HSKDYNYDPD
     YGRYDSSATL DEMKQYNVQW SNSIVVGHGN VGAGVDWQKQ TTEPGTGYVT DGYDQRNTGL
     YLTGLQQLGD FTFEGAARSD DNSEFGRHGT WQTSAGWEFI EGYRFIASYG TSYKAPNLGQ
     LHGYYGNSNL DPEQSKQWEG AFEGLTAGVN WRVSGYRNDI DDMIDYDPHT EKYFNEGKVR
     IKGVEATANF DTGPLAHTLS YDMVDSRNAI TDKPLARRSK QQVKYQLDWQ VYDFDWGLTY
     HYLGTRYDTD YVTYQPVKMG GVSLWDLAVS YPITSQLTVR GKIANRFDKD YETVYGYATA
     GREYTLSGSY TF
 
 
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