CBIM_LIMRD
ID CBIM_LIMRD Reviewed; 248 AA.
AC A5VM74;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=Lreu_1709;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ83948.1; -; Genomic_DNA.
DR RefSeq; WP_003669133.1; NZ_AZDD01000019.1.
DR AlphaFoldDB; A5VM74; -.
DR SMR; A5VM74; -.
DR STRING; 557436.Lreu_1709; -.
DR EnsemblBacteria; ABQ83948; ABQ83948; Lreu_1709.
DR GeneID; 66471886; -.
DR KEGG; lre:Lreu_1709; -.
DR PATRIC; fig|557436.17.peg.631; -.
DR eggNOG; COG0310; Bacteria.
DR HOGENOM; CLU_052508_3_0_9; -.
DR OMA; ANVFSMG; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001991; 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..31
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT CHAIN 32..248
FT /note="Cobalt transport protein CbiM"
FT /id="PRO_5000251465"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 75..95
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 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01462"
SQ SEQUENCE 248 AA; 26992 MW; 79A58D6C40E1D022 CRC64;
MLKVIKKYRK FITFLMIGLV YTLAYPATAH AMHIMEGMLP PRWCIFWYAV SLPFFIYGLY
RMYKIVNSGV PNAKVMLALC GAFVFVLSSL KLPSVTGSCS HPTGVGLGTV LFGPGVMSVL
GVIVLLFQAL LLAHGGITTL GANEFSMTIV GPIVGYAVWK LCRAMKVSRS VSLFLCAMFA
DWSTYVTTAF QLAIVFPDPN GGVAAALIKF LSIYAITQIP LAIAEGLLTV IVYNLVISND
LWKESALQ