ECFA2_LACP3
ID ECFA2_LACP3 Reviewed; 288 AA.
AC Q035B3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=cbiO1, ecfA';
GN OrderedLocusNames=LSEI_2473;
OS Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=321967;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC B-441;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
RN [2]
RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBSTRATES, AND EXPRESSION IN
RP L.LACTIS.
RC STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC B-441;
RX PubMed=18931129; DOI=10.1128/jb.01208-08;
RA Rodionov D.A., Hebbeln P., Eudes A., ter Beek J., Rodionova I.A.,
RA Erkens G.B., Slotboom D.J., Gelfand M.S., Osterman A.L., Hanson A.D.,
RA Eitinger T.;
RT "A novel class of modular transporters for vitamins in prokaryotes.";
RL J. Bacteriol. 191:42-51(2009).
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 including 5-formyltetrahydrofolate and thiamine.
CC Expression of the complex plus FolT or ThiT in Lactococcus lactis
CC subsp. cremoris (strain NZ9000) allows 5-formyltetrahydrofolate or
CC thiamine uptake respectively; 5-formyltetrahydrofolate or thiamine are
CC not taken up in the absence of FolT/ThiT or the EcfA1A2T complex.
CC Deenergized L.lactis subsp. cremoris (treated with 2-deoxyglucose) do
CC not take up substrate. {ECO:0000255|HAMAP-Rule:MF_01710,
CC ECO:0000269|PubMed:18931129}.
CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC complex probably composed of 2 membrane-embedded substrate-binding
CC proteins (S component), 2 ATP-binding proteins (A component) and 2
CC transmembrane proteins (T component). This complex interacts with a
CC number of substrate-specific components, including FolT and ThiT for 5-
CC formyltetrahydrofolate and thiamine respectively.
CC {ECO:0000269|PubMed:18931129}.
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; CP000423; ABJ71209.1; -; Genomic_DNA.
DR RefSeq; WP_003567503.1; NC_008526.1.
DR RefSeq; YP_807651.1; NC_008526.1.
DR AlphaFoldDB; Q035B3; -.
DR SMR; Q035B3; -.
DR STRING; 321967.LSEI_2473; -.
DR EnsemblBacteria; ABJ71209; ABJ71209; LSEI_2473.
DR GeneID; 61270573; -.
DR KEGG; lca:LSEI_2473; -.
DR PATRIC; fig|321967.11.peg.2427; -.
DR HOGENOM; CLU_000604_1_22_9; -.
DR OMA; PKYLFCD; -.
DR Proteomes; UP000001651; 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:0022857; F:transmembrane transporter activity; IEA:UniProt.
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; Hydrolase; Membrane; Nucleotide-binding;
KW Transport.
FT CHAIN 1..288
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA2"
FT /id="PRO_0000287945"
FT DOMAIN 3..246
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT ACT_SITE 171
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 288 AA; 31235 MW; 019210785A2B613B CRC64;
MDITFDHVSF TYQAGTPFAG DGIKDVSGVI RDGSYTAIIG HTGSGKSTIL QHLNALLKPT
SGTVTIGDKV ITNETNNKNL KPLRQKVGMV FQFAENQLFE QTVAKDIAFG PQNFGVSEKD
ALALADKMVK MVGLPHDVLE KSPFDLSGGQ MRRVAIAGVL AMQPEVLVLD EPTAGLDPSG
RHEMMQMFEQ LHREQGQTIV LVTHQMDDVA DYADTVWVMA EGKLIKTGTP REIFADPAWL
KANQLGLPKT AQLAQQLAAK GFHFDPQPLT ESELADQLVP QIGGGQRG
