CBIM_THEVB
ID CBIM_THEVB Reviewed; 257 AA.
AC Q8DG81;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=tll2442;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01462}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01462}.
CC -!- SIMILARITY: Belongs to the CbiM family. {ECO:0000255|HAMAP-
CC Rule:MF_01462}.
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DR EMBL; BA000039; BAC09994.1; -; Genomic_DNA.
DR RefSeq; NP_683232.2; NC_004113.1.
DR AlphaFoldDB; Q8DG81; -.
DR SMR; Q8DG81; -.
DR STRING; 197221.22296170; -.
DR EnsemblBacteria; BAC09994; BAC09994; BAC09994.
DR KEGG; tel:tll2442; -.
DR PATRIC; fig|197221.4.peg.2566; -.
DR eggNOG; COG0310; Bacteria.
DR OMA; ANVFSMG; -.
DR OrthoDB; 1632785at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000440; 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 inner membrane; Cell membrane; Cobalamin biosynthesis; Cobalt;
KW Cobalt transport; Ion transport; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT CHAIN 34..257
FT /note="Cobalt transport protein CbiM"
FT /id="PRO_0000411150"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
SQ SEQUENCE 257 AA; 27303 MW; DB3BF83B10315299 CRC64;
MVKPTQAKRY ASLGAIALLT TSLVVASPNP ALAMHISEGF LPLGWAVGWW LAFLPFLAWG
LWSLQQQIKQ HSESVLLVAL AGAYAFVVSS LKIPSVTGSC SHPIGIALGA ILFRPPLMAV
LGTLVLLFQS LLIAHGGLTT LGANAFSMAV VGPWLAWLTY CGVSRLRVKP AIALFAASFI
SNVGTYTLTS LQLALAFPDS VGGLATSFAK FGTLFAVTQI PLAISEGLLT VLVWNWLTTY
CVAELQALRL LPQEELP
