CBIO_RHOCB
ID CBIO_RHOCB Reviewed; 280 AA.
AC O68106; D5AUZ6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cobalt import ATP-binding protein CbiO;
DE EC=7.2.2.-;
DE AltName: Full=Energy-coupling factor transporter ATP-binding protein CbiO;
DE Short=ECF transporter A component CbiO;
GN Name=cbiO; Synonyms=cbiO2; OrderedLocusNames=RCAP_rcc02034;
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. Presumably responsible for energy coupling to the transport
CC system. {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:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AF010496; AAC16196.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85778.1; -; Genomic_DNA.
DR PIR; T03543; T03543.
DR RefSeq; WP_013067757.1; NC_014034.1.
DR PDB; 5X3X; X-ray; 2.79 A; A/B/a/b=1-280.
DR PDB; 5X40; X-ray; 1.45 A; A/B=1-280.
DR PDBsum; 5X3X; -.
DR PDBsum; 5X40; -.
DR AlphaFoldDB; O68106; -.
DR SMR; O68106; -.
DR STRING; 272942.RCAP_rcc02034; -.
DR TCDB; 3.A.1.23.8; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE85778; ADE85778; RCAP_rcc02034.
DR GeneID; 31490896; -.
DR KEGG; rcp:RCAP_rcc02034; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_1_22_5; -.
DR OMA; TRIRMHQ; -.
DR OrthoDB; 1752365at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006824; P:cobalt ion transport; IDA:UniProtKB.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR InterPro; IPR005876; Co_trans_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01166; cbiO; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
KW Cobalamin biosynthesis; Cobalt; Cobalt transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..280
FT /note="Cobalt import ATP-binding protein CbiO"
FT /id="PRO_0000092057"
FT DOMAIN 5..240
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 19..28
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5X3X"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:5X40"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 173..188
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:5X40"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5X40"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:5X40"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:5X40"
SQ SEQUENCE 280 AA; 29436 MW; FB24F5C6E3233FBB CRC64;
MTPILAAEAL TYAFPGGVKA LDDLSLAVPQ GESLAILGPN GAGKSTLLLH LNGTLRPQSG
RVLLGGTATG HSRKDLTDWR RRVGLVLQDA DDQLFAATVF EDVSFGPLNL GLSEAEARAR
VEEALAALSI SDLRDRPTHM LSGGQKRRVA IAGAVAMRPE VLLLDEPTAG LDLAGTEQLL
TLLHGLRAAG MTLVFSTHDV ELAAALADRV ALFRTGRVLA EGAAAAVLSD RATLAQGGLR
PPLVIDLALS RARSRPFGPR SALPRTRDAL AAQMAGWTRR
