ECFA2_LACLM
ID ECFA2_LACLM Reviewed; 288 AA.
AC A2RI02;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA2 {ECO:0000255|HAMAP-Rule:MF_01710};
DE Short=ECF transporter A component EcfA2 {ECO:0000255|HAMAP-Rule:MF_01710};
DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01710};
DE AltName: Full=ECF transporter A component EcfA';
GN Name=ecfA2 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO2, ecfA';
GN OrderedLocusNames=llmg_0288;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [2]
RP SUBUNIT, SUBCELLULAR LOCATION, TRANSPORT SUBSTRATES, EXPRESSION IN E.COLI
RP AND L.LACTIS, AND FUNCTION.
RC STRAIN=MG1363;
RX PubMed=21135102; DOI=10.1074/jbc.m110.199224;
RA ter Beek J., Duurkens R.H., Erkens G.B., Slotboom D.J.;
RT "Quaternary structure and functional unit of energy coupling factor (ECF)-
RT type transporters.";
RL J. Biol. Chem. 286:5471-5475(2011).
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. In this organism these probably include biotin,
CC thiamine precursor, niacin, pantothenic acid, queuosine precursor,
CC riboflavin and thiamine. Uptake of niacin or riboflavin into
CC proteosomes containing EcfA1A2T and Niax or RibU has been demonstrated.
CC Uptake requires hydrolyzable Mg-ATP and is substrate-specific; NiaX-
CC containing proteosomes did not transport riboflavin.
CC {ECO:0000255|HAMAP-Rule:MF_01710, ECO:0000269|PubMed:21135102}.
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). In L.lactis forms a stable complex with EcfA'
CC and EcfT and substrate-binding components. In E.coli forms a stable
CC complex with EcfA, EcfT and individually with 3 tested substrate-
CC binding components (BioY, NiaX and ThiT) with a stoichiometry of
CC 1.1:1:1. The core ECF complex interacts with a number of substrate-
CC specific binding components, including BioY, BioY2, HmpT, NiaX, PanT,
CC QueT, RibU and ThiT. {ECO:0000255|HAMAP-Rule:MF_01710,
CC ECO:0000269|PubMed:21135102}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21135102};
CC Peripheral membrane protein {ECO:0000305|PubMed:21135102}.
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; AM406671; CAL96895.1; -; Genomic_DNA.
DR RefSeq; WP_011834359.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; A2RI02; -.
DR SMR; A2RI02; -.
DR STRING; 416870.llmg_0288; -.
DR EnsemblBacteria; CAL96895; CAL96895; llmg_0288.
DR KEGG; llm:llmg_0288; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_1_22_9; -.
DR OMA; PKYLFCD; -.
DR PhylomeDB; A2RI02; -.
DR BioCyc; LLAC416870:LLMG_RS01505-MON; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
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; IPR030946; EcfA2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR04521; ECF_ATPase_2; 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 ATP-binding; Cell membrane; Cobalt; Cobalt transport; Hydrolase;
KW Ion transport; Membrane; Nucleotide-binding; Transport.
FT CHAIN 1..288
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA2"
FT /id="PRO_0000287958"
FT DOMAIN 2..244
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
SQ SEQUENCE 288 AA; 31624 MW; 593C296543A391E6 CRC64;
MIKFEKVNYT YQPNSPFASR ALFDIDLEVK KGSYTALIGH TGSGKSTLLQ HLNGLLQPTE
GKVTVGDIVV SSTSKQKEIK PVRKKVGVVF QFPESQLFEE TVLKDVAFGP QNFGIPKEKA
EKIAAEKLEM VGLADEFWEK SPFELSGGQM RRVAIAGILA MEPEVLVLDE PTAGLDPKAR
IEMMQLFESI HQSGQTVVLV THLMDDVADY ADYVYLLEKG HIISCGTPSD VFQEVDFLKA
HELGVPKATH FADQLQKTGA VAFEKLPITR AELVTLLTSL SVNSGGEN
