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MALC_STRPN
ID   MALC_STRPN              Reviewed;         435 AA.
AC   P0A4N1; Q04698;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Maltodextrin transport system permease protein MalC;
GN   Name=malC; OrderedLocusNames=SP_2109;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8478935; DOI=10.1006/jmbi.1993.1202;
RA   Puyet A., Espinosa M.;
RT   "Structure of the maltodextrin-uptake locus of Streptococcus pneumoniae.
RT   Correlation to the Escherichia coli maltose regulon.";
RL   J. Mol. Biol. 230:800-811(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC       maltodextrin; probably responsible for the translocation of the
CC       substrate across the membrane.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. MalFG subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA26926.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L08611; AAA26926.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE005672; AAK76168.1; -; Genomic_DNA.
DR   PIR; G95246; G95246.
DR   RefSeq; WP_001808667.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P0A4N1; -.
DR   SMR; P0A4N1; -.
DR   STRING; 170187.SP_2109; -.
DR   EnsemblBacteria; AAK76168; AAK76168; SP_2109.
DR   KEGG; spn:SP_2109; -.
DR   eggNOG; COG1175; Bacteria.
DR   OMA; WYAYAMI; -.
DR   PhylomeDB; P0A4N1; -.
DR   BioCyc; SPNE170187:G1FZB-2197-MON; -.
DR   BRENDA; 2.4.1.25; 1960.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR030156; MalF-like.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   PANTHER; PTHR47314:SF1; PTHR47314:SF1; 2.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Sugar transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..435
FT                   /note="Maltodextrin transport system permease protein MalC"
FT                   /id="PRO_0000060094"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          195..423
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   CONFLICT        236..239
FT                   /note="LLPW -> PSSL (in Ref. 1; AAA26926)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        434
FT                   /note="D -> E (in Ref. 1; AAA26926)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   435 AA;  48302 MW;  32259E3E44AFC4DF CRC64;
     MKGVNMEKQQ PSKAALLSII PGLGQIYNKQ KAKGFIFLGV TIVFVLYFLA LATPELSNLI
     TLGDKPGRDN SLFMLIRGAF HLIFVIVYVL FYFSNIKDAH TIAKRINNGI PVPRTLKDMI
     KGIYENGFPY LLIIPSYVAM TFAIIFPVIV TLMIAFTNYD FQHLPPNKLL DWVGLTNFTN
     IWSLSTFRSA FGSVLSWTII WALAASTLQI VIGIFTAIIA NQPFIKGKRI FGVIFLLPWA
     VPAFITILTF SNMFNDSVGA INTQVLPILA KFLPFLDGAL IPWKTDPTWT KIALIMMQGW
     LGFPYIYVLT LGILQSIPND LYEAAYIDGA NAWQKFRNIT FPMILAVAAP TLISQYTFNF
     NNFSIMYLFN GGGPGSVGGG AGSTDILISW IYRLTTGTSP QYSMAAAVTL IISIIVISIS
     MIAFKKLHAF DMEDV
 
 
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