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   27-MAR-2024, entry version 140.
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; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   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.TM_0222; -.
DR   TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily.
DR   PaxDb; 243274-THEMA_03615; -.
DR   EnsemblBacteria; AAD35314; AAD35314; TM_0222.
DR   KEGG; tma:TM0222; -.
DR   eggNOG; COG1122; Bacteria.
DR   InParanoid; Q9WY65; -.
DR   OrthoDB; 9784332at2; -.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR43553:SF1; ABC TRANSPORTER I FAMILY MEMBER 11, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43553; HEAVY METAL TRANSPORTER; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//