(data stored in ACNUC9543 zone)

SWISSPROT: BTUB_YERPA

ID   BTUB_YERPA              Reviewed;         625 AA.
AC   Q1CBU1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   08-MAY-2019, entry version 85.
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};
GN   OrderedLocusNames=YPA_0112;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Involved in the active translocation of vitamin B12
CC       (cyanocobalamin) across the outer membrane to the periplasmic
CC       space. It derives its energy for transport by interacting with the
CC       trans-periplasmic membrane protein TonB. {ECO:0000255|HAMAP-
CC       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
CC       (TC 1.B.14.3.1) subfamily. {ECO:0000255|HAMAP-Rule:MF_01531}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABG12081.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000308; ABG12081.1; ALT_INIT; Genomic_DNA.
DR   SMR; Q1CBU1; -.
DR   EnsemblBacteria; ABG12081; ABG12081; YPA_0112.
DR   KEGG; ypa:YPA_0112; -.
DR   HOGENOM; HOG000269547; -.
DR   KO; K16092; -.
DR   Proteomes; UP000001971; 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:cobalamin-transporting ATPase 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;
DR   PRODOM; Q1CBU1.
DR   SWISS-2DPAGE; Q1CBU1.
KW   Calcium; Cell outer membrane; Complete proteome; Ion transport;
KW   Membrane; Metal-binding; Porin; Signal; TonB box; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   SIGNAL        1     21       {ECO:0000255|HAMAP-Rule:MF_01531}.
FT   CHAIN        22    625       Vitamin B12 transporter BtuB.
FT                                /FTId=PRO_5000115719.
FT   TRANSMEM    163    170       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    174    183       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    189    200       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    223    233       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    238    254       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    271    285       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    287    304       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    317    333       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    336    345       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    363    379       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    381    391       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    395    410       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    413    427       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    445    454       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    460    469       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    484    501       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    505    520       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    528    540       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    546    561       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    569    583       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    596    607       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   TRANSMEM    613    625       Beta stranded. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   REGION      113    117       Cobalamin-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   REGION      255    257       Cobalamin-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   REGION      526    529       Cobalamin-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   MOTIF        31     38       TonB box.
FT   MOTIF       608    625       TonB C-terminal box.
FT   METAL       204    204       Calcium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   METAL       217    217       Calcium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   METAL       219    219       Calcium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   METAL       219    219       Calcium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   METAL       221    221       Calcium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   METAL       221    221       Calcium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   METAL       255    255       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01531}.
FT   METAL       256    256       Calcium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   METAL       256    256       Calcium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
FT   METAL       269    269       Calcium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01531}.
SQ   SEQUENCE   625 AA;  69808 MW;  9BFE0DCDEBD76216 CRC64;
     MTIKKYTLLT ALSVTAFSGW AQGNNTTDNN DEMVVTANRF PQPKSSVLAP VDVVTRADID
     RWQSTNINDV LRRLPGVDIA QDGGMGQRSS LFIRGTNSSH VLVLIDGVRL NQAGITGASD
     LSQIPISLVQ RIEYIRGPRS AVYGSDAIGG VINILTGRDK PGTTLSAGLG SNGYQTYDGS
     TQQKLGEDTT VTLAGNYTYS KGYDVVAGMP GAGGPRQPDR DGFMGKMLWA GLEHQFNEQF
     NGFARVYGFD NRSDYDGYTN YSNPLALIDT RKLSSRTYDT GLRYKNGIYA SQFIASYNRT
     KDYNYSPLFG QHDITASLDE AEQYNLQWGN TFQLTNGMIS AGADWQEQRT ERKSSNQNTT
     ADFTQHNTGI YLTGQQQISD VTLEGAVRSD DNSQFGWHST WQTSAGWEFI DGYRLIGSYG
     TAYKAPNLMQ LYSAYGGNAN LKPEESKQWE GGVEGLTGPL TWRLSAYRND IDQLIDYSNL
     TNGYFNINKA TIKGVEWTGS FDTGPLSHQV TLEYLDPRNA DTHEILVRRA KQQVKYQLDW
     QVADLDWSVT YQYLGQRYDK DYSTYPEETV ELGGVSLWDL AVSYPVTSHL TVRGRIANLF
     DKDYEMVYGY QTPGREYYFT GSYNF
//

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