CBIM_RHOCB
ID CBIM_RHOCB Reviewed; 222 AA.
AC D5AUZ9; O68103;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Cobalt transport protein CbiM;
DE AltName: Full=Energy-coupling factor transporter probable substrate-capture protein CbiM;
DE Short=ECF transporter S component CbiM;
GN Name=cbiM; OrderedLocusNames=RCAP_rcc02037;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=9256491; DOI=10.1073/pnas.94.17.9384;
RA Vlcek C., Paces V., Maltsev N., Paces J., Haselkorn R., Fonstein M.;
RT "Sequence of a 189-kb segment of the chromosome of Rhodobacter capsulatus
RT SB1003.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9384-9388(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP PROTEIN SEQUENCE OF 1-6, FUNCTION IN COBALT TRANSPORT, SUBUNIT, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF MET-1; HIS-2; ILE-3; MET-4; GLU-5; GLY-6;
RP TYR-7; LEU-8 AND PRO-9.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20868747; DOI=10.1016/j.resmic.2010.09.010;
RA Siche S., Neubauer O., Hebbeln P., Eitinger T.;
RT "A bipartite S unit of an ECF-type cobalt transporter.";
RL Res. Microbiol. 161:824-829(2010).
RN [4]
RP FUNCTION IN COBALT TRANSPORT, SUBSTRATES, SUBUNIT, AND EXPRESSION IN
RP E.COLI.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=16352848; DOI=10.1128/jb.188.1.317-327.2006;
RA Rodionov D.A., Hebbeln P., Gelfand M.S., Eitinger T.;
RT "Comparative and functional genomic analysis of prokaryotic nickel and
RT cobalt uptake transporters: evidence for a novel group of ATP-binding
RT cassette transporters.";
RL J. Bacteriol. 188:317-327(2006).
CC -!- FUNCTION: Part of the energy-coupling factor (ECF) transporter complex
CC CbiMNOQ involved in cobalt import. The complex confers cobalt uptake
CC upon expression in E.coli; can also transport nickel with a very low
CC affinity. A Cbi(MN) fusion protein has about 70% import capacity, but
CC the holo-Cbi(MN)QO complex cannot be isolated, suggesting CbiN may
CC destabilize it. {ECO:0000269|PubMed:16352848,
CC ECO:0000269|PubMed:20868747}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
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. Subcomplexes
CC composed of CbiMQO can be isolated from membranes but the CbiN subunit
CC is not isolated in association with them, suggesting it is only loosely
CC associated. Expression of just CbiMN in E.coli confers some cobalt
CC uptake. {ECO:0000269|PubMed:16352848, ECO:0000269|PubMed:20868747}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:20868747}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:20868747}.
CC -!- SIMILARITY: Belongs to the CbiM family. {ECO:0000305}.
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DR EMBL; AF010496; AAC16193.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85781.1; -; Genomic_DNA.
DR PIR; T03540; T03540.
DR RefSeq; WP_013067760.1; NC_014034.1.
DR PDB; 5X3X; X-ray; 2.79 A; M/m=1-222.
DR PDBsum; 5X3X; -.
DR AlphaFoldDB; D5AUZ9; -.
DR SMR; D5AUZ9; -.
DR STRING; 272942.RCAP_rcc02037; -.
DR TCDB; 3.A.1.23.8; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE85781; ADE85781; RCAP_rcc02037.
DR GeneID; 31490899; -.
DR KEGG; rcp:RCAP_rcc02037; -.
DR eggNOG; COG0310; Bacteria.
DR HOGENOM; CLU_052508_3_0_5; -.
DR OMA; ANVFSMG; -.
DR OrthoDB; 1632785at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:UniProtKB.
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 GO; GO:0006824; P:cobalt ion transport; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cobalamin biosynthesis;
KW Cobalt; Cobalt transport; Direct protein sequencing; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..222
FT /note="Cobalt transport protein CbiM"
FT /id="PRO_0000411082"
FT TOPO_DOM 1..8
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..74
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..133
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 1
FT /note="M->MA,MM: No cobalt uptake, Cbi(MN) protein
FT accumulates normally."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 2
FT /note="H->C,N,Q,S: No cobalt uptake, Cbi(MN) protein
FT accumulates normally."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 2
FT /note="H->D: No cobalt uptake, Cbi(MN) protein accumulates
FT normally but has altered mobility during gel
FT electrophoresis."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 3
FT /note="Missing: No cobalt uptake, Cbi(MN) protein
FT accumulates normally."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 4
FT /note="M->A,S: Cobalt uptake normal for Cbi(MN) construct."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 4
FT /note="Missing: No cobalt uptake, Cbi(MN) protein
FT accumulates normally."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 5
FT /note="Missing: No cobalt uptake, Cbi(MN) protein
FT accumulates normally."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 6
FT /note="Missing: No cobalt uptake, Cbi(MN) protein
FT accumulates normally."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 7
FT /note="Missing: Very small amounts of cobalt uptake,
FT Cbi(MN) protein accumulates normally."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 8
FT /note="Missing: No cobalt uptake, Cbi(MN) protein
FT accumulates normally."
FT /evidence="ECO:0000269|PubMed:20868747"
FT MUTAGEN 9
FT /note="Missing: No cobalt uptake, Cbi(MN) protein
FT accumulates normally."
FT /evidence="ECO:0000269|PubMed:20868747"
FT HELIX 10..37
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:5X3X"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:5X3X"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 110..132
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 137..163
FT /evidence="ECO:0007829|PDB:5X3X"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 171..206
FT /evidence="ECO:0007829|PDB:5X3X"
SQ SEQUENCE 222 AA; 22636 MW; 603AB726DDFE1BBF CRC64;
MHIMEGYLPV THAIGWSLAA GPFVVAGAVK IRKIVAERPE ARMTLAASGA FAFVLSALKI
PSVTGSCSHP TGTGLGAVVF GPSVMAVLGV IVLLFQALLL AHGGLTTLGA NAFSMAIVGP
WVAWGVYKLA GKAGASMAVA VFLAAFLGDL ATYVTTSLQL ALAYPDPVSG FLGAALKFGS
VFALTQIPLA IAEGFLTVIV VDALAGKVDD KDKLRILAGE AR
