CBIM_ACESD
ID CBIM_ACESD Reviewed; 241 AA.
AC E3PSD4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 53.
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=CLOST_1668;
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
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; FP565809; CBH21788.1; -; Genomic_DNA.
DR AlphaFoldDB; E3PSD4; -.
DR SMR; E3PSD4; -.
DR STRING; 1511.CLOST_1668; -.
DR EnsemblBacteria; CBH21788; CBH21788; CLOST_1668.
DR KEGG; cst:CLOST_1668; -.
DR eggNOG; COG0310; Bacteria.
DR HOGENOM; CLU_052508_3_0_9; -.
DR OMA; ANVFSMG; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000007041; 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..241
FT /note="Cobalt transport protein CbiM"
FT /id="PRO_0000411139"
FT TRANSMEM 30..50
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 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
SQ SEQUENCE 241 AA; 25737 MW; 800BB378133E0C70 CRC64;
MKKIKIISFS VAYLILLTPI YASAMHIMEG FLPPLWAAIW SVISLPFIVG GFSKIKKITD
ESPNMKLLLG LVGAFVFVLS ALKLPSVTGS TSHPTGVGLG TIIFGPLPMA VIGLIVLIFQ
ALLLAHGGIT TLGANVFSMA IVGPFAGYFI FKAIKDKNRS LAVFLAAMLA DLITYIVTSL
QLALAHPDAV NGIVGSFTKF MGIFAITQIP LAIGEGILTL IVYNLLVEYQ KEGGFNLEKT
H