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ECFA2_STRT2
ID   ECFA2_STRT2             Reviewed;         280 AA.
AC   Q5M244;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 120.
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};
GN   Name=ecfA2 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO2;
GN   OrderedLocusNames=stu2008;
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-97 AND GLU-171.
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; AAV61602.1; -; Genomic_DNA.
DR   RefSeq; WP_002947774.1; NC_006448.1.
DR   AlphaFoldDB; Q5M244; -.
DR   SMR; Q5M244; -.
DR   STRING; 264199.stu2008; -.
DR   TCDB; 3.A.1.25.6; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; AAV61602; AAV61602; stu2008.
DR   GeneID; 66899734; -.
DR   KEGG; stl:stu2008; -.
DR   eggNOG; COG1122; Bacteria.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; FVFQRPA; -.
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:0016787; F:hydrolase activity; 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; 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   Reference proteome; Transport.
FT   CHAIN           1..280
FT                   /note="Energy-coupling factor transporter ATP-binding
FT                   protein EcfA2"
FT                   /id="PRO_0000288009"
FT   DOMAIN          3..245
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"
FT   MUTAGEN         97
FT                   /note="Q->A: No effect on ATPase, 10-fold decrease in
FT                   riboflavin uptake; when associated with A-90 in EcfA1."
FT                   /evidence="ECO:0000269|PubMed:23359690"
FT   MUTAGEN         171
FT                   /note="E->Q: 10-fold decrease in ATPase and riboflavin
FT                   uptake; when associated with Q-163 in EcfA1."
FT                   /evidence="ECO:0000269|PubMed:23359690"
SQ   SEQUENCE   280 AA;  30942 MW;  34136CAFCBCC6B9E CRC64;
     MGISLENVSY TYQSGTPFER RALFDMTVTI KDGSYTAFIG HTGSGKSTIM QLLNGLYLPT
     SGQVKVDDTI INSQSKNKEI KPIRKKVGLV FQFPESQLFA ETVLEDIAFG PQNFGVSKEE
     AEQRALESLR LVGLSDELRD QNPFDLSGGQ MRRVAIAGIL AMQPDILVLD EPTAGLDPQG
     RKELMSLFKQ LHLSGITIVL VTHLMDDVAD YATAVNVMEK GRLVLSGTPK DVFQKVAFLK
     EKQLGVPKIT EFALQLQEKG YSFESLPITI EEFVEVLVHG
 
 
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