CBIM1_METBF
ID CBIM1_METBF Reviewed; 231 AA.
AC Q46D59;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Putative cobalt transport protein CbiM 1 {ECO:0000255|HAMAP-Rule:MF_01462};
DE AltName: Full=Energy-coupling factor transporter probable substrate-capture protein CbiM 1 {ECO:0000255|HAMAP-Rule:MF_01462};
DE Short=ECF transporter S component CbiM 1 {ECO:0000255|HAMAP-Rule:MF_01462};
GN Name=cbiM1 {ECO:0000255|HAMAP-Rule:MF_01462}; OrderedLocusNames=Mbar_A1216;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70183.1; -; Genomic_DNA.
DR RefSeq; WP_011306230.1; NC_007355.1.
DR AlphaFoldDB; Q46D59; -.
DR SMR; Q46D59; -.
DR STRING; 269797.Mbar_A1216; -.
DR EnsemblBacteria; AAZ70183; AAZ70183; Mbar_A1216.
DR GeneID; 3624563; -.
DR KEGG; mba:Mbar_A1216; -.
DR eggNOG; arCOG02248; Archaea.
DR HOGENOM; CLU_052508_3_0_2; -.
DR OMA; IAWGVIC; -.
DR OrthoDB; 94360at2157; -.
DR UniPathway; UPA00148; -.
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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..231
FT /note="Putative cobalt transport protein CbiM 1"
FT /id="PRO_0000411158"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 41..61
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 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
SQ SEQUENCE 231 AA; 25029 MW; 309B6BE11827AF10 CRC64;
MHIFEGFLPG PWWQIWWILS IPVFAYGIFR LNKLVKEKPE VLPLIAVSGA VIFVLSSLKL
PSVTGSTSHP TGTGMAVILF GPAITSVLSA IVLLYQALFL AHGGITTFGA NLMSMGIIGP
FVAYAIYKTM MRLNVNFYVS AFVTATLADW VTYVVTSTQL ALAFPANPGG VEGSLVAFLS
VFAITQIPLA ILEASLITLL FKYVLQAKGD LMVRLDVLTD SQVRKLKETK A