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MESD_LEUME
ID   MESD_LEUME              Reviewed;         722 AA.
AC   Q10418;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Mesentericin-Y105 transport/processing ATP-binding protein MesD;
DE            EC=3.4.22.-;
DE            EC=7.-.-.-;
GN   Name=mesD;
OS   Leuconostoc mesenteroides.
OG   Plasmid pHY30.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=1245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Y105;
RX   PubMed=7551032; DOI=10.1099/13500872-141-7-1637;
RA   Fremaux C., Hechard A., Cenatiempo Y.;
RT   "Mesentericin Y105 gene clusters in Leuconostoc mesenteroides Y105.";
RL   Microbiology 141:1637-1645(1995).
CC   -!- FUNCTION: Involved in the export process of the bacteriocin
CC       mesentericin-Y105.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; X81803; CAA57402.1; -; Genomic_DNA.
DR   PIR; S52205; S52205.
DR   AlphaFoldDB; Q10418; -.
DR   SMR; Q10418; -.
DR   MEROPS; C39.001; -.
DR   TCDB; 3.A.1.112.8; the atp-binding cassette (abc) superfamily.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043214; F:ABC-type bacteriocin transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005897; Pept_C39_ABC_bacteriocin.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF03412; Peptidase_C39; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   TIGRFAMs; TIGR01193; bacteriocin_ABC; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bacteriocin transport; Cell membrane; Hydrolase; Membrane;
KW   Nucleotide-binding; Plasmid; Protease; Protein transport; Thiol protease;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..722
FT                   /note="Mesentericin-Y105 transport/processing ATP-binding
FT                   protein MesD"
FT                   /id="PRO_0000092502"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        518..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          16..143
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   DOMAIN          173..455
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          489..722
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
FT   ACT_SITE        22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   BINDING         522..529
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   722 AA;  79916 MW;  8452E899F8C02E16 CRC64;
     MVKTPMFHKK IDYISQVDER DCGVAALAMI LAHYKTRLSL AKLRDLAKTD MEGTTALGIV
     KAANALDFET MPIQADLSLF DKKDLPYPFI AHVIKEGKYP HYYVVYGMKG DQLLIADPDN
     TVGKTKMTKA HFNEEWTGVS IFIAPNPTYK PTKEKKRSLT SFIPVITRQK LLVINIVIAA
     LLVTLVSILG SYYLQGIIDT YIPNNMKNTL GIVSLGLIFA YVIQQLLSYA RDYLLIVMGQ
     RLSIDIILSY IKHIFELPMS FFATRRTGEI VSRFTDANAI IEALASTMLS VFLDLGILVI
     VGTVLVVQNS TLFLISLIAI PAYALVVWLF MRPFSKMNND QMQAGSMLSS SIIEDINGVE
     TIKALNSEAT AYHKIDHEFV TYLEKSFVYA KTEAVQNAIK SLLQLSLNVV ILWVGAQLVM
     TNKISVGQLI TYNALLGFFT DPLQNIINLQ TKLQQASVAN NRLNEVYLVD SEFKDSHQMT
     EKITPNSSLV ADHITYKYGF GAPAIDDVSL TITAGEKIAL VGISGSGKST LVKLLVNFFQ
     PESGTISLGP TPLANLDKHE LRGHINYLPQ EPFIFSGSIM ENLLLGAKPG TTQEDIIRAV
     EIAEIKDDIE KMSQGFGTEL AESGNISGGQ KQRIALARAI LVDSPVLILD ESTSNLDVLT
     EKKIIDNLMK LTEKTIIFVA HRLTISQRVD RILTMQSGKI IEDGTHDTLL KAGGFYASLF
     NH
 
 
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