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SAPD_HAEIN
ID   SAPD_HAEIN              Reviewed;         349 AA.
AC   P45288;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Peptide transport system ATP-binding protein SapD;
GN   Name=sapD; OrderedLocusNames=HI_1641;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Involved in a peptide intake transport system that plays a
CC       role in the resistance to antimicrobial peptides. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; L42023; AAC23288.1; -; Genomic_DNA.
DR   PIR; D64134; D64134.
DR   RefSeq; NP_439783.1; NC_000907.1.
DR   RefSeq; WP_005693649.1; NC_000907.1.
DR   AlphaFoldDB; P45288; -.
DR   SMR; P45288; -.
DR   STRING; 71421.HI_1641; -.
DR   EnsemblBacteria; AAC23288; AAC23288; HI_1641.
DR   KEGG; hin:HI_1641; -.
DR   PATRIC; fig|71421.8.peg.1717; -.
DR   eggNOG; COG4172; Bacteria.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   OMA; PHGRVKA; -.
DR   PhylomeDB; P45288; -.
DR   BioCyc; HINF71421:G1GJ1-1658-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; 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; IPR013563; Oligopep_ABC_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..349
FT                   /note="Peptide transport system ATP-binding protein SapD"
FT                   /id="PRO_0000092967"
FT   DOMAIN          1..259
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   349 AA;  39478 MW;  25FD3241F1570D7A CRC64;
     MALLDICNLN IEIQTSNGRI KIVDGVNLSL NEGEISGLVG ESGSGKSLIA KVICNAIKEN
     WIITADRFRF HDVELLKLSP NKRRKLVGKE ISMIFQNPLS CLDPSRKIGK QLIQNIPNWT
     FKNKWWKWFG WKKRRAIELL HRVGIKDHRD IMASYPNELT EGEGQKVMIA MAVANQPRLL
     IADEPTNALE STTALQVFRL LSSMNQNQGT TILLTSNDIK SISEWCDQIS VLYCGQNTES
     APTEILIESP HHPYTQALIN AVPDFTQPLG FKTKLGTLEG TAPILEQMPI GCRLGPRCPF
     AQKKCMEKPR RLKIKQHEFS CHYPINLREK NFKEKTTATP FILNCKGNE
 
 
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