ECFA3_CLOP1
ID ECFA3_CLOP1 Reviewed; 285 AA.
AC Q0TUN8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA3 {ECO:0000255|HAMAP-Rule:MF_01710};
DE Short=ECF transporter A component EcfA3 {ECO:0000255|HAMAP-Rule:MF_01710};
DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01710};
GN Name=ecfA3 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO1;
GN OrderedLocusNames=CPF_0188;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-265.
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RG New York structural genomix research consortium (NYSGXRC);
RT "Structure of Cbio1 from Clostridium perfringens: part of the ABC
RT transporter complex CbiONQ.";
RL Submitted (MAR-2009) to the PDB data bank.
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. {ECO:0000255|HAMAP-Rule:MF_01710}.
CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC complex composed of 2 membrane-embedded substrate-binding proteins (S
CC component), 2 ATP-binding proteins (A component) and 2 transmembrane
CC proteins (T component). {ECO:0000255|HAMAP-Rule:MF_01710}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01710};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01710}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy-coupling
CC factor EcfA family. {ECO:0000255|HAMAP-Rule:MF_01710}.
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DR EMBL; CP000246; ABG82220.1; -; Genomic_DNA.
DR RefSeq; WP_003457507.1; NC_008261.1.
DR PDB; 3GFO; X-ray; 2.30 A; A=2-265.
DR PDBsum; 3GFO; -.
DR AlphaFoldDB; Q0TUN8; -.
DR SMR; Q0TUN8; -.
DR STRING; 195103.CPF_0188; -.
DR DNASU; 4201231; -.
DR EnsemblBacteria; ABG82220; ABG82220; CPF_0188.
DR GeneID; 29572690; -.
DR KEGG; cpf:CPF_0188; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_1_22_9; -.
DR OMA; DIVPLYC; -.
DR OrthoDB; 1752365at2; -.
DR EvolutionaryTrace; Q0TUN8; -.
DR Proteomes; UP000001823; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006824; P:cobalt ion transport; IEA:InterPro.
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.
DR PROSITE; PS51246; CBIO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Transport.
FT CHAIN 1..285
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA3"
FT /id="PRO_0000287932"
FT DOMAIN 6..242
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:3GFO"
FT STRAND 20..30
FT /evidence="ECO:0007829|PDB:3GFO"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:3GFO"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:3GFO"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3GFO"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:3GFO"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3GFO"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 174..191
FT /evidence="ECO:0007829|PDB:3GFO"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:3GFO"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:3GFO"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 231..242
FT /evidence="ECO:0007829|PDB:3GFO"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:3GFO"
SQ SEQUENCE 285 AA; 32114 MW; AF1AF8960CB06495 CRC64;
MEDYILKVEE LNYNYSDGTH ALKGINMNIK RGEVTAILGG NGVGKSTLFQ NFNGILKPSS
GRILFDNKPI DYSRKGIMKL RESIGIVFQD PDNQLFSASV YQDVSFGAVN MKLPEDEIRK
RVDNALKRTG IEHLKDKPTH CLSFGQKKRV AIAGVLVMEP KVLILDEPTA GLDPMGVSEI
MKLLVEMQKE LGITIIIATH DIDIVPLYCD NVFVMKEGRV ILQGNPKEVF AEKEVIRKVN
LRLPRIGHLM EILKEKDGFV FDELDLTIGQ ARKTINSWKN KIFND
