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POTA_STRSV
ID   POTA_STRSV              Reviewed;         385 AA.
AC   A3CMQ7;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Spermidine/putrescine import ATP-binding protein PotA {ECO:0000255|HAMAP-Rule:MF_01726};
DE            EC=7.6.2.11 {ECO:0000255|HAMAP-Rule:MF_01726};
GN   Name=potA {ECO:0000255|HAMAP-Rule:MF_01726}; OrderedLocusNames=SSA_1048;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
CC   -!- FUNCTION: Part of the ABC transporter complex PotABCD involved in
CC       spermidine/putrescine import. Responsible for energy coupling to the
CC       transport system. {ECO:0000255|HAMAP-Rule:MF_01726}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP
CC         + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.;
CC         EC=7.6.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01726};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PotA),
CC       two transmembrane proteins (PotB and PotC) and a solute-binding protein
CC       (PotD). {ECO:0000255|HAMAP-Rule:MF_01726}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01726};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01726}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Spermidine/putrescine importer (TC 3.A.1.11.1) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01726}.
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DR   EMBL; CP000387; ABN44462.1; -; Genomic_DNA.
DR   RefSeq; WP_011836889.1; NC_009009.1.
DR   RefSeq; YP_001035012.1; NC_009009.1.
DR   AlphaFoldDB; A3CMQ7; -.
DR   SMR; A3CMQ7; -.
DR   STRING; 388919.SSA_1048; -.
DR   EnsemblBacteria; ABN44462; ABN44462; SSA_1048.
DR   KEGG; ssa:SSA_1048; -.
DR   PATRIC; fig|388919.9.peg.994; -.
DR   eggNOG; COG3842; Bacteria.
DR   HOGENOM; CLU_000604_1_1_9; -.
DR   OMA; IHVMRFN; -.
DR   OrthoDB; 1200451at2; -.
DR   Proteomes; UP000002148; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0015417; F:ABC-type polyamine transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013611; Transp-assoc_OB_typ2.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08402; TOBE_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; SSF50331; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51305; POTA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..385
FT                   /note="Spermidine/putrescine import ATP-binding protein
FT                   PotA"
FT                   /id="PRO_0000286314"
FT   DOMAIN          6..238
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01726"
SQ   SEQUENCE   385 AA;  44268 MW;  096D62D4154F522D CRC64;
     MKKPIIEFKN VSKVFEDNNT VVLKDINFEL EEGKFYTLLG SSGSGKSTIL NIIAGLLDAT
     DGDIFLDGVR INDIPTNKRD VHTVFQSYAL FPHMNVFENV AFPLRLRKVD KKEIQERVTE
     VLKMVQLEGF ERRSIRKLSG GQRQRVAIAR AIINQPRVVL LDEPLSALDL KLRTDMQYEL
     RELQQRLGIT FVFVTHDQEE ALAMSDWIFV MNDGEIVQSG TPVDIYDEPI NHFVATFIGE
     SNILPGKMIE DYLVEFNGKR FEAVDGGMRP NESVEVVIRP EDLRITLPEE GKLQVKVDTQ
     LFRGVHYEII AYDELGNEWM IHSTRKAIVG EEIGLHFEPE DIHIMRLNET EEEFDARIEE
     YVEVEEQEAG LINAIEEERD EENNL
 
 
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