CBIM_DESRM
ID CBIM_DESRM Reviewed; 250 AA.
AC A4J832;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Dred_2731;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000612; ABO51235.1; -; Genomic_DNA.
DR RefSeq; WP_011879032.1; NC_009253.1.
DR AlphaFoldDB; A4J832; -.
DR SMR; A4J832; -.
DR STRING; 349161.Dred_2731; -.
DR EnsemblBacteria; ABO51235; ABO51235; Dred_2731.
DR KEGG; drm:Dred_2731; -.
DR eggNOG; COG0310; Bacteria.
DR HOGENOM; CLU_052508_3_0_9; -.
DR OMA; ANVFSMG; -.
DR OrthoDB; 1632785at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001556; 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..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT CHAIN 25..250
FT /note="Cobalt transport protein CbiM"
FT /id="PRO_5000231537"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
SQ SEQUENCE 250 AA; 27124 MW; 105A0A74526A2D2A CRC64;
MKYWGTALLG AFCVFFFTPN TAYAMHIAEG FLPAGWCLFW LALSVPFVFW GIRSIHISLR
GNPHLKMLLG LAGAFVFVLS ALKIPSVTGS CSHPTGVGLG AILFGPAVMS VLGCIVLLFQ
ALLLAHGGIT TLGANVFSMG VMGPLVSYGV YQLLKKRNTK VAVFLAASLG NMTTYMVTSL
QLAMAFPDKT GNLLVSFFKF MSIFAITQIP LAITEGLLTV FVFNLLNNYR EELYPGLPKE
ERSGPYDFVN
