ECFA2_THEMA
ID ECFA2_THEMA Reviewed; 266 AA.
AC Q9WY65;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA2;
DE Short=ECF transporter A component EcfA2;
DE EC=7.-.-.-;
GN Name=ecfA2; Synonyms=ecfA, ecfA'; OrderedLocusNames=TM_0222;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=18540059; DOI=10.1107/s1744309108013778;
RA Ethayathulla A.S., Bessho Y., Shinkai A., Padmanabhan B., Singh T.P.,
RA Kaur P., Yokoyama S.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of the putative ABC transporter ATP-binding protein from Thermotoga
RT maritima.";
RL Acta Crystallogr. F 64:498-500(2008).
RN [3]
RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION,
RP EXPRESSION IN E.COLI, ATP-BINDING, AND X-RAY CRYSTALLOGRAPHY (2.7
RP ANGSTROMS) OF 2-266 IN COMPLEX WITH ADP.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23359690; DOI=10.1073/pnas.1217361110;
RA Karpowich N.K., Wang D.N.;
RT "Assembly and mechanism of a group II ECF transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013).
CC -!- FUNCTION: ATP-binding (A) component of a common energy-coupling factor
CC (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF
CC transporter provides the energy necessary to transport a number of
CC different substrates (Probable). Expression of the complex plus RibU in
CC E.coli allows riboflavin uptake; uptake does not occur in the absence
CC of RibU or the EcfA1A2T complex. {ECO:0000269|PubMed:23359690,
CC ECO:0000305}.
CC -!- SUBUNIT: Forms a heterodimer with EcfA1. Forms a stable energy-coupling
CC factor (ECF) transporter complex composed of 2 membrane-embedded
CC substrate-binding proteins (S component, RibU, BioY), 2 ATP-binding
CC proteins (A component) and 2 transmembrane proteins (T component) upon
CC coexpression in E.coli. Stable subcomplexes with both A plus T
CC components can also be isolated. This complex interacts with at least 2
CC substrate-specific components, BioY and RibU.
CC {ECO:0000269|PubMed:23359690}.
CC -!- INTERACTION:
CC Q9WY65; Q9X1Z1: ecfA1; NbExp=2; IntAct=EBI-16160779, EBI-16160756;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:23359690}; Peripheral membrane protein
CC {ECO:0000305|PubMed:23359690}.
CC -!- MISCELLANEOUS: Structure 4HLU is probably in the open state.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy-coupling
CC factor EcfA family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35314.1; -; Genomic_DNA.
DR PIR; A72401; A72401.
DR RefSeq; NP_228037.1; NC_000853.1.
DR RefSeq; WP_004082907.1; NZ_CP011107.1.
DR PDB; 2YZ2; X-ray; 2.30 A; A/B=1-266.
DR PDB; 4HLU; X-ray; 2.70 A; A/B=2-266.
DR PDB; 4ZIR; X-ray; 3.00 A; A=2-266.
DR PDBsum; 2YZ2; -.
DR PDBsum; 4HLU; -.
DR PDBsum; 4ZIR; -.
DR AlphaFoldDB; Q9WY65; -.
DR SMR; Q9WY65; -.
DR DIP; DIP-61612N; -.
DR IntAct; Q9WY65; 1.
DR STRING; 243274.THEMA_03615; -.
DR TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAD35314; AAD35314; TM_0222.
DR KEGG; tma:TM0222; -.
DR eggNOG; COG1122; Bacteria.
DR InParanoid; Q9WY65; -.
DR OMA; DIVPLYC; -.
DR OrthoDB; 1752365at2; -.
DR EvolutionaryTrace; Q9WY65; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IGI:UniProtKB.
DR GO; GO:0032218; P:riboflavin transport; IGI: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; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..266
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA2"
FT /id="PRO_0000092115"
FT DOMAIN 3..238
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 220..266
FT /note="Required for heterodimer formation"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 43..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 20..30
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4ZIR"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:2YZ2"
FT TURN 103..107
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:2YZ2"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:2YZ2"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:4HLU"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:2YZ2"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:2YZ2"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2YZ2"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:2YZ2"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:2YZ2"
SQ SEQUENCE 266 AA; 30233 MW; EB146157FC21EB4F CRC64;
MRIEVVNVSH IFHRGTPLEK KALENVSLVI NEGECLLVAG NTGSGKSTLL QIVAGLIEPT
SGDVLYDGER KKGYEIRRNI GIAFQYPEDQ FFAERVFDEV AFAVKNFYPD RDPVPLVKKA
MEFVGLDFDS FKDRVPFFLS GGEKRRVAIA SVIVHEPDIL ILDEPLVGLD REGKTDLLRI
VEKWKTLGKT VILISHDIET VINHVDRVVV LEKGKKVFDG TRMEFLEKYD PRFFTSKMLV
MRRLVLKGED PFSMSDDELL ERVCNS
