ID BTUF_ECOLI Reviewed; 266 AA.
AC P37028; P77436;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 24-JAN-2024, entry version 176.
DE RecName: Full=Vitamin B12-binding protein {ECO:0000255|HAMAP-Rule:MF_01000};
DE Flags: Precursor;
GN Name=btuF; Synonyms=yadT; OrderedLocusNames=b0158, JW0154;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 208.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-6 (PRECURSOR PROTEIN), PROTEIN SEQUENCE OF 23-27,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11790740; DOI=10.1128/jb.184.3.706-717.2002;
RA Cadieux N., Bradbeer C., Reeger-Schneider E., Koester W., Mohanty A.K.,
RA Wiener M.C., Kadner R.J.;
RT "Identification of the periplasmic cobalamin-binding protein BtuF of
RT Escherichia coli.";
RL J. Bacteriol. 184:706-717(2002).
RN [6] {ECO:0007744|PDB:1N2Z}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-266 IN COMPLEX WITH
RP CYANOCOB(III)ALAMIN, AND SUBUNIT.
RX PubMed=12475936; DOI=10.1073/pnas.262659699;
RA Borths E.L., Locher K.P., Lee A.T., Rees D.C.;
RT "The structure of Escherichia coli BtuF and binding to its cognate ATP
RT binding cassette transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16642-16647(2002).
RN [7] {ECO:0007744|PDB:1N4A, ECO:0007744|PDB:1N4D}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-266 IN COMPLEX WITH
RP CYANOCOB(III)ALAMIN.
RX PubMed=12468528; DOI=10.1074/jbc.m212239200;
RA Karpowich N.K., Huang H.H., Smith P.C., Hunt J.F.;
RT "Crystal structures of the BtuF periplasmic-binding protein for vitamin B12
RT suggest a functionally important reduction in protein mobility upon ligand
RT binding.";
RL J. Biol. Chem. 278:8429-8434(2003).
CC -!- FUNCTION: Part of the ABC transporter complex BtuCDF involved in
CC vitamin B12 import. Binds vitamin B12 and delivers it to the
CC periplasmic surface of BtuC. {ECO:0000255|HAMAP-Rule:MF_01000,
CC ECO:0000269|PubMed:11790740}.
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:0000255|HAMAP-Rule:MF_01000, ECO:0000269|PubMed:12468528,
CC ECO:0000269|PubMed:12475936}.
CC -!- INTERACTION:
CC P37028; P06609: btuC; NbExp=10; IntAct=EBI-1118724, EBI-1033427;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01000,
CC ECO:0000269|PubMed:11790740}.
CC -!- MISCELLANEOUS: Vitamin B12 is bound in a deep cleft formed at the
CC interface between the two lobes of BtuF. {ECO:0000269|PubMed:12475936}.
CC -!- SIMILARITY: Belongs to the BtuF family. {ECO:0000255|HAMAP-
CC Rule:MF_01000, ECO:0000305}.
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DR EMBL; U70214; AAB08588.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73269.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96735.2; -; Genomic_DNA.
DR PIR; F64739; F64739.
DR RefSeq; NP_414700.1; NC_000913.3.
DR RefSeq; WP_001129927.1; NZ_STEB01000032.1.
DR PDB; 1N2Z; X-ray; 2.00 A; A/B=22-266.
DR PDB; 1N4A; X-ray; 2.00 A; A/B=23-266.
DR PDB; 1N4D; X-ray; 3.00 A; A/B=23-266.
DR PDB; 2QI9; X-ray; 2.60 A; F=22-266.
DR PDB; 4DBL; X-ray; 3.49 A; E/J=22-266.
DR PDB; 4FI3; X-ray; 3.47 A; F=22-266.
DR PDB; 5M29; X-ray; 1.50 A; A/B=22-266.
DR PDB; 5M2Q; X-ray; 1.70 A; A/B=22-266.
DR PDB; 5M34; X-ray; 1.60 A; A/B=22-266.
DR PDB; 5M3B; X-ray; 1.50 A; A/B=22-266.
DR PDB; 5OVW; X-ray; 2.65 A; A/B/C/D/E/F=22-266.
DR PDBsum; 1N2Z; -.
DR PDBsum; 1N4A; -.
DR PDBsum; 1N4D; -.
DR PDBsum; 2QI9; -.
DR PDBsum; 4DBL; -.
DR PDBsum; 4FI3; -.
DR PDBsum; 5M29; -.
DR PDBsum; 5M2Q; -.
DR PDBsum; 5M34; -.
DR PDBsum; 5M3B; -.
DR PDBsum; 5OVW; -.
DR AlphaFoldDB; P37028; -.
DR SMR; P37028; -.
DR BioGRID; 4261861; 279.
DR ComplexPortal; CPX-2105; Cobalamin ABC transporter complex.
DR DIP; DIP-11194N; -.
DR IntAct; P37028; 5.
DR MINT; P37028; -.
DR STRING; 511145.b0158; -.
DR jPOST; P37028; -.
DR PaxDb; 511145-b0158; -.
DR ABCD; P37028; 7 sequenced antibodies.
DR EnsemblBacteria; AAC73269; AAC73269; b0158.
DR GeneID; 75202027; -.
DR GeneID; 947574; -.
DR KEGG; ecj:JW0154; -.
DR KEGG; eco:b0158; -.
DR PATRIC; fig|1411691.4.peg.2122; -.
DR EchoBASE; EB2238; -.
DR eggNOG; COG0614; Bacteria.
DR HOGENOM; CLU_038034_2_5_6; -.
DR InParanoid; P37028; -.
DR OMA; WQGINLE; -.
DR OrthoDB; 6495095at2; -.
DR PhylomeDB; P37028; -.
DR BioCyc; EcoCyc:EG12334-MONOMER; -.
DR BioCyc; MetaCyc:EG12334-MONOMER; -.
DR BRENDA; 7.6.2.8; 2026.
DR EvolutionaryTrace; P37028; -.
DR PRO; PR:P37028; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990191; C:cobalamin transport complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0031419; F:cobalamin binding; IDA:EcoliWiki.
DR GO; GO:0015889; P:cobalamin transport; IDA:EcoCyc.
DR CDD; cd01144; BtuF; 1.
DR DisProt; DP02169; -.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR HAMAP; MF_01000; BtuF; 1.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR InterPro; IPR023544; ABC_transptr_vit_B12-bd.
DR NCBIfam; NF038402; TroA_like; 1.
DR PANTHER; PTHR42860; VITAMIN B12-BINDING PROTEIN; 1.
DR PANTHER; PTHR42860:SF1; VITAMIN B12-BINDING PROTEIN; 1.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:11790740"
FT CHAIN 23..266
FT /note="Vitamin B12-binding protein"
FT /id="PRO_0000003497"
FT DOMAIN 25..266
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT BINDING 50
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000,
FT ECO:0000269|PubMed:12468528, ECO:0007744|PDB:1N4A"
FT BINDING 242..246
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000,
FT ECO:0000269|PubMed:12468528, ECO:0000269|PubMed:12475936,
FT ECO:0007744|PDB:1N2Z, ECO:0007744|PDB:1N4A"
FT SITE 72
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000,
FT ECO:0000305|PubMed:12475936"
FT SITE 202
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01000,
FT ECO:0000305|PubMed:12475936"
FT DISULFID 183..259
FT CONFLICT 208
FT /note="S -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5M29"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5M29"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:5M29"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:5M29"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:5M29"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:5M29"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:5M29"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1N4A"
FT HELIX 129..150
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5OVW"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5M2Q"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5M29"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5M29"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:5M29"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1N2Z"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:1N2Z"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1N4A"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:5M29"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:5M29"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:5M34"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:5M29"
SQ SEQUENCE 266 AA; 29367 MW; 480F2E620ACD6EA1 CRC64;
MAKSLFRALV ALSFLAPLWL NAAPRVITLS PANTELAFAA GITPVGVSSY SDYPPQAQKI
EQVSTWQGMN LERIVALKPD LVIAWRGGNA ERQVDQLASL GIKVMWVDAT SIEQIANALR
QLAPWSPQPD KAEQAAQSLL DQYAQLKAQY ADKPKKRVFL QFGINPPFTS GKESIQNQVL
EVCGGENIFK DSRVPWPQVS REQVLARSPQ AIVITGGPDQ IPKIKQYWGE QLKIPVIPLT
SDWFERASPR IILAAQQLCN ALSQVD
//
