CBIQ_RHOCB
ID CBIQ_RHOCB Reviewed; 244 AA.
AC D5AUZ7; O68105;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Cobalt transport protein CbiQ;
DE AltName: Full=Energy-coupling factor transporter transmembrane protein CbiQ;
DE Short=ECF transporter T component CbiQ;
GN Name=cbiQ; Synonyms=cbiQ2; OrderedLocusNames=RCAP_rcc02035;
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 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).
RN [4]
RP FUNCTION IN COBALT TRANSPORT, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
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. {ECO:0000269|PubMed:16352848, 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 {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CbiQ family. {ECO:0000305}.
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DR EMBL; AF010496; AAC16195.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85779.1; -; Genomic_DNA.
DR PIR; T03542; T03542.
DR PDB; 5X3X; X-ray; 2.79 A; Q/q=1-244.
DR PDBsum; 5X3X; -.
DR AlphaFoldDB; D5AUZ7; -.
DR SMR; D5AUZ7; -.
DR STRING; 272942.RCAP_rcc02035; -.
DR TCDB; 3.A.1.23.8; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE85779; ADE85779; RCAP_rcc02035.
DR KEGG; rcp:RCAP_rcc02035; -.
DR eggNOG; COG0619; Bacteria.
DR HOGENOM; CLU_056469_5_2_5; -.
DR OMA; IAMMMYR; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006824; P:cobalt ion transport; IDA:UniProtKB.
DR InterPro; IPR003339; ABC/ECF_trnsptr_transmembrane.
DR InterPro; IPR012809; ECF_CbiQ.
DR Pfam; PF02361; CbiQ; 1.
DR TIGRFAMs; TIGR02454; ECF_T_CbiQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cobalamin biosynthesis;
KW Cobalt; Cobalt transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..244
FT /note="Cobalt transport protein CbiQ"
FT /id="PRO_0000411084"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:5X3X"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 20..36
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:5X3X"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:5X3X"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 98..122
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:5X3X"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 139..168
FT /evidence="ECO:0007829|PDB:5X3X"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 175..205
FT /evidence="ECO:0007829|PDB:5X3X"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:5X3X"
SQ SEQUENCE 244 AA; 25881 MW; BAE536630747C9AF CRC64;
MSIASIDRVA AQGRWRNRPL AEKCLIGLGF LALAVTVPPF PGAVLVTVAI LAFTFLGARV
PLRFWAAVAV LPLGFLTTGA AVLLIQIGPD GIGLAPQGPA KAAALVMRAS AATCCLLFLA
TTTPAADLLS GLRRWRVPAE LIEIALLTYR FVFILAEEAA AMTTAQRARL GHATRRRWLR
STAQVIAALL PRALDRARRL ETGLAARNWQ GEMRVLSTRP AASPLVLGLI LTLQAAILAA
GVLL
