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ECFA1_LACP3
ID   ECFA1_LACP3             Reviewed;         278 AA.
AC   Q035B2;
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 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=cbiO2, ecfA;
GN   OrderedLocusNames=LSEI_2474;
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) does
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; ABJ71210.1; -; Genomic_DNA.
DR   RefSeq; WP_003580999.1; NC_008526.1.
DR   RefSeq; YP_807652.1; NC_008526.1.
DR   AlphaFoldDB; Q035B2; -.
DR   SMR; Q035B2; -.
DR   STRING; 321967.LSEI_2474; -.
DR   EnsemblBacteria; ABJ71210; ABJ71210; LSEI_2474.
DR   GeneID; 61270574; -.
DR   KEGG; lca:LSEI_2474; -.
DR   PATRIC; fig|321967.11.peg.2428; -.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; RMKDFDA; -.
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: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; 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..278
FT                   /note="Energy-coupling factor transporter ATP-binding
FT                   protein EcfA1"
FT                   /id="PRO_0000287946"
FT   DOMAIN          5..239
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT   ACT_SITE        165
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   278 AA;  30482 MW;  D6FA19AEB1F75F67 CRC64;
     MGNVIRVQHL NYTYPEAKQQ ALTDVSFDVA KGEWLAIIGH NGSGKSTLAK NLNGLLAPES
     GTVQVAGMTL SEETVWDIRA KVGIVFQNPD NQFVGATVAD DVAFGLENRG VPRPEMIKRV
     DEALDRVGMT AFADREPARL SGGQKQRVAI AGIVAQRPEI IILDESTSML DPAGRQEVLG
     VIRELKDELG LTVLSITHDI DEAAEAHRII LLNDGKINEI GTPSEIFSHG MELLRLGLDV
     PYSEKLKDAL AQRGIAMPKD YMDNERLVDY LWTLHSTM
 
 
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