ID A0A068QZD2_9GAMM Unreviewed; 277 AA.
AC A0A068QZD2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Vitamin B12-binding protein {ECO:0000256|HAMAP-Rule:MF_01000};
GN Name=btuF {ECO:0000256|HAMAP-Rule:MF_01000,
GN ECO:0000313|EMBL:CDG20283.1};
GN ORFNames=XPG1_0628 {ECO:0000313|EMBL:CDG20283.1};
OS Xenorhabdus poinarii G6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG20283.1, ECO:0000313|Proteomes:UP000032735};
RN [1] {ECO:0000313|EMBL:CDG20283.1, ECO:0000313|Proteomes:UP000032735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G6 {ECO:0000313|EMBL:CDG20283.1,
RC ECO:0000313|Proteomes:UP000032735};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01000}.
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:0000256|HAMAP-Rule:MF_01000}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01000}.
CC -!- SIMILARITY: Belongs to the BtuF family. {ECO:0000256|HAMAP-
CC Rule:MF_01000}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01000}.
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DR EMBL; FO704551; CDG20283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068QZD2; -.
DR STRING; 1354304.XPG1_0628; -.
DR KEGG; xpo:XPG1_0628; -.
DR HOGENOM; CLU_038034_2_5_6; -.
DR OrthoDB; 6495095at2; -.
DR Proteomes; UP000032735; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0015889; P:cobalamin transport; IEA:UniProtKB-UniRule.
DR CDD; cd01144; BtuF; 1.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01000};
KW Periplasm {ECO:0000256|HAMAP-Rule:MF_01000};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01000};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01000}.
FT DOMAIN 34..277
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000259|PROSITE:PS50983"
FT BINDING 61
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01000"
FT SITE 83
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01000"
FT SITE 213
FT /note="Important for BtuC binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01000"
FT DISULFID 194..270
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01000"
SQ SEQUENCE 277 AA; 30967 MW; E176B94C3076923C CRC64;
MQLFLKIIPS QSVWWVFSFL LSVFNAPLYA AATRVISLAP STTELAYAAG LGDQLVAVSA
YSDYPAAAKK LEQVADWQGI NVERIIALKP DLILAWRGGN PQRPLAQLAA LGIPIFYSDI
QKIDDVATEL EQLAVYNRHP DTARQSAENI RNKFKQLKQH YAHVTPKPVF LQFGMNPIFT
SSSHTIQSEI VSVCGGKNIF ADSPVPWPQV NREQVLTRKP EILIIGGTEA QKQRVADFWR
PHMNIHIIAL NDDWFSRAGP RIILAAEQLC QQLNDAK
//
