CBIM_ANOFW
ID CBIM_ANOFW Reviewed; 250 AA.
AC B7GLU2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Cobalt transport protein CbiM {ECO:0000255|HAMAP-Rule:MF_01462};
DE AltName: Full=Energy-coupling factor transporter probable substrate-capture protein CbiM {ECO:0000255|HAMAP-Rule:MF_01462};
DE Short=ECF transporter S component CbiM {ECO:0000255|HAMAP-Rule:MF_01462};
DE Flags: Precursor;
GN Name=cbiM {ECO:0000255|HAMAP-Rule:MF_01462}; OrderedLocusNames=Aflv_2184;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
CC -!- FUNCTION: Part of the energy-coupling factor (ECF) transporter complex
CC CbiMNOQ involved in cobalt import. {ECO:0000255|HAMAP-Rule:MF_01462}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01462}.
CC -!- SUBUNIT: Forms an energy-coupling factor (ECF) transporter complex
CC composed of an ATP-binding protein (A component, CbiO), a transmembrane
CC protein (T component, CbiQ) and 2 possible substrate-capture proteins
CC (S components, CbiM and CbiN) of unknown stoichimetry.
CC {ECO:0000255|HAMAP-Rule:MF_01462}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01462};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01462}.
CC -!- SIMILARITY: Belongs to the CbiM family. {ECO:0000255|HAMAP-
CC Rule:MF_01462}.
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DR EMBL; CP000922; ACJ34543.1; -; Genomic_DNA.
DR RefSeq; WP_012575721.1; NC_011567.1.
DR AlphaFoldDB; B7GLU2; -.
DR SMR; B7GLU2; -.
DR STRING; 491915.Aflv_2184; -.
DR EnsemblBacteria; ACJ34543; ACJ34543; Aflv_2184.
DR KEGG; afl:Aflv_2184; -.
DR PATRIC; fig|491915.6.peg.2243; -.
DR eggNOG; COG0310; Bacteria.
DR HOGENOM; CLU_052508_3_0_9; -.
DR OMA; ANVFSMG; -.
DR OrthoDB; 1632785at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000742; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01462; CbiM; 1.
DR InterPro; IPR018024; CbiM.
DR InterPro; IPR002751; CbiM/NikMN.
DR PANTHER; PTHR43627; PTHR43627; 1.
DR Pfam; PF01891; CbiM; 1.
DR TIGRFAMs; TIGR00123; cbiM; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cobalamin biosynthesis; Cobalt; Cobalt transport;
KW Ion transport; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT CHAIN 28..250
FT /note="Cobalt transport protein CbiM"
FT /id="PRO_0000411135"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
SQ SEQUENCE 250 AA; 27150 MW; 1525F1D50AA42E86 CRC64;
MKKPLFFIAS ACVTIYILFA LSPSVYAMHI MEGFLPWQWA LVWWLLFLPF FLVGMRNVAR
LMRQRPEVKL LLALATAFTF VLSALKIPSV TGSSSHPTGT GLGALLFGPF VMTVIGTAVL
LFQALLLAHG GVTTLGANAF SMAVVGPLVA YVLFSLCKKF GVSTRVSVFL AAMMADLATY
VMTSIQLALA FPDATSGVWG AFLKFASIFA VTQIPLAITE GLLTVVVWNF LHTYSKRELT
ILQQKGATIE