ECFA1_LACLM
ID ECFA1_LACLM Reviewed; 277 AA.
AC A2RI01;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710};
DE Short=ECF transporter A component EcfA {ECO:0000255|HAMAP-Rule:MF_01710};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_01710};
GN Name=ecfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO1, ecfA;
GN OrderedLocusNames=llmg_0287;
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; CAL96894.1; -; Genomic_DNA.
DR RefSeq; WP_011675310.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; A2RI01; -.
DR SMR; A2RI01; -.
DR STRING; 416870.llmg_0287; -.
DR TCDB; 3.A.1.25.4; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; CAL96894; CAL96894; llmg_0287.
DR KEGG; llm:llmg_0287; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_1_22_9; -.
DR OMA; RMKDFDA; -.
DR PhylomeDB; A2RI01; -.
DR BioCyc; LLAC416870:LLMG_RS01500-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 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; IPR030947; EcfA_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR04520; ECF_ATPase_1; 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; Membrane; Nucleotide-binding; Translocase;
KW Transport.
FT CHAIN 1..277
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA1"
FT /id="PRO_0000287957"
FT DOMAIN 5..240
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
SQ SEQUENCE 277 AA; 30931 MW; 4F00F35365A22FD2 CRC64;
MNKILEVENL VFKYEKESDV NQLNGVSFSI TKGEWVSIIG QNGSGKSTTA RLIDGLFEEF
EGIVKIDGER LTAENVWNLR RKIGMVFQNP DNQFVGATVE DDVAFGMENQ GIPREEMIKR
VDEALLAVNM LDFKTREPAR LSGGQKQRVA VAGIIALRPE IIILDESTSM LDPTGRSEIM
RVIHEIKDKY HLTVLSITHD LDEAASSDRI LVMRAGEIIK EAAPSELFAT SEDMVEIGLD
VPFSSNLMKD LRTNGFDLPE KYLSEDELVE LLADKLG
