ID   A0A0N0IAT5_9GAMM        Unreviewed;       281 AA.
AC   A0A0N0IAT5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Vitamin B12-binding protein {ECO:0000256|HAMAP-Rule:MF_01000};
GN   Name=btuF {ECO:0000256|HAMAP-Rule:MF_01000};
GN   ORFNames=M992_1199 {ECO:0000313|EMBL:KPD03322.1};
OS   Moellerella wisconsensis ATCC 35017.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Moellerella.
OX   NCBI_TaxID=1354267 {ECO:0000313|EMBL:KPD03322.1, ECO:0000313|Proteomes:UP000053226};
RN   [1] {ECO:0000313|EMBL:KPD03322.1, ECO:0000313|Proteomes:UP000053226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35017 {ECO:0000313|EMBL:KPD03322.1,
RC   ECO:0000313|Proteomes:UP000053226};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (JUL-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPD03322.1}.
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DR   EMBL; LGAA01000011; KPD03322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0IAT5; -.
DR   OrthoDB; 6495095at2; -.
DR   Proteomes; UP000053226; Unassembled WGS sequence.
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; PTHR30535:SF37; MOLYBDATE-BINDING PROTEIN MOLA; 1.
DR   PANTHER; PTHR30535; 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   Reference proteome {ECO:0000313|Proteomes:UP000053226};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01000};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01000}.
FT   DOMAIN          36..281
FT                   /note="Fe/B12 periplasmic-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50983"
FT   BINDING         63
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01000"
FT   SITE            85
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01000"
FT   SITE            216
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01000"
FT   DISULFID        197..273
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01000"
SQ   SEQUENCE   281 AA;  31327 MW;  7F436ED486120CF9 CRC64;
     MHKIHVRIPP IAAVIFTLLF TSIFSITVSY AEVKQRIISL SPANTELAYA AGMGDSLIAV
     SAYSDYPPEA KKLEQVADWQ GINLERIIAL KPDLILAWRG GNPQRPLDQI AALGIPVIYF
     DPNSINEIIA AINTLAEYSP HPDIAKKSTQ LLQQQLDDLH QKYQNNTLNK PVFIQLGTQP
     LFTAGGKTLQ NEIVALCGGQ NIFANSQIPW PQVSREQVLV RQPEYIIIAG SEDQKSIIER
     FWQPQMKAKI ISLNQDWFHR AGPRSLLAAQ QLCAQINSIN Q
//