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ECFA1_STRT2
ID   ECFA1_STRT2             Reviewed;         276 AA.
AC   Q5M243;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710};
DE            Short=ECF transporter A component EcfA1 {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;
GN   OrderedLocusNames=stu2009;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
RN   [2]
RP   FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION,
RP   EXPRESSION IN E.COLI, AND MUTAGENESIS OF GLN-90 AND GLU-163.
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=23359690; DOI=10.1073/pnas.1217361110;
RA   Karpowich N.K., Wang D.N.;
RT   "Assembly and mechanism of a group II ECF transporter.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013).
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 (By similarity). Expression of the complex plus
CC       RibU in de-energized E.coli allows riboflavin uptake.
CC       {ECO:0000255|HAMAP-Rule:MF_01710, ECO:0000269|PubMed:23359690}.
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) upon coexpression of the components in E.coli.
CC       May be able to interact with more than 1 S component at a time.
CC       {ECO:0000255|HAMAP-Rule:MF_01710, ECO:0000269|PubMed:23359690}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23359690};
CC       Peripheral membrane protein {ECO:0000305|PubMed:23359690}.
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; CP000023; AAV61603.1; -; Genomic_DNA.
DR   RefSeq; WP_002947776.1; NC_006448.1.
DR   AlphaFoldDB; Q5M243; -.
DR   SMR; Q5M243; -.
DR   STRING; 264199.stu2009; -.
DR   TCDB; 3.A.1.25.6; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; AAV61603; AAV61603; stu2009.
DR   GeneID; 66899735; -.
DR   KEGG; stl:stu2009; -.
DR   eggNOG; COG1122; Bacteria.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; RMKDFDA; -.
DR   Proteomes; UP000001170; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0032217; F:riboflavin transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0032218; P:riboflavin transport; IMP:UniProtKB.
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;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..276
FT                   /note="Energy-coupling factor transporter ATP-binding
FT                   protein EcfA1"
FT                   /id="PRO_0000288010"
FT   DOMAIN          2..237
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT   MUTAGEN         90
FT                   /note="Q->A: No effect on ATPase, 10-fold decrease in
FT                   riboflavin uptake; when associated with A-97 in EcfA2."
FT                   /evidence="ECO:0000269|PubMed:23359690"
FT   MUTAGEN         163
FT                   /note="E->Q: 10-fold decrease in ATPase and riboflavin
FT                   uptake; when associated with Q-171 in EcfA2."
FT                   /evidence="ECO:0000269|PubMed:23359690"
SQ   SEQUENCE   276 AA;  30946 MW;  1FAB24FE62661345 CRC64;
     MIEIKNLKFK YNQDQTSYTL NDVSFHVKHG EWLSIVGHNG SGKSTTARLI GGLLVADSGQ
     IIVDGQELTE ETVWDIRDKI GMVFQNPDNQ FVGATVEDDV AFGLENKGLP YKEMVSRVQE
     ALSFVGMMDF KDREPARLSG GQKQRVAIAG IIAMRPSILI LDEATSMLDP EGRQELIQYI
     EDIRQQYGMT VLSITHDLDE VAMSNRVLVL KQGKVESISS PRELFSRGSE LVDLGLDIPF
     SALLTQKLKN QGLIDCEGYL TEKELVEQLW EYLSKM
 
 
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