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NIST_LACLL
ID   NIST_LACLL              Reviewed;         600 AA.
AC   Q03203;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Nisin transport ATP-binding protein NisT;
GN   Name=nisT;
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=6F3;
RX   PubMed=1482192; DOI=10.1128/aem.58.11.3730-3743.1992;
RA   Engelke G., Gutowski-Eckel Z., Hammelmann M., Entian K.-D.;
RT   "Biosynthesis of the lantibiotic nisin: genomic organization and membrane
RT   localization of the NisB protein.";
RL   Appl. Environ. Microbiol. 58:3730-3743(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NIZO R5;
RX   PubMed=7689965; DOI=10.1111/j.1432-1033.1993.tb18143.x;
RA   Kuipers O.P., Beerthuyzen M.M., Siezen R.J., de Vos W.M.;
RT   "Characterization of the nisin gene cluster nisABTCIPR of Lactococcus
RT   lactis. Requirement of expression of the nisA and nisI genes for
RT   development of immunity.";
RL   Eur. J. Biochem. 216:281-291(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RC   STRAIN=ATCC 11454 / DSM 20729 / LMG 7930 / NCDO 496 / NCIMB 8586 / Berridge
RC   X 13;
RX   PubMed=1905517; DOI=10.1128/aem.57.4.1181-1188.1991;
RA   Steen M.T., Chung Y.J., Hansen J.N.;
RT   "Characterization of the nisin gene as part of a polycistronic operon in
RT   the chromosome of Lactococcus lactis ATCC 11454.";
RL   Appl. Environ. Microbiol. 57:1181-1188(1991).
CC   -!- FUNCTION: Probably implicated in the export process of the lantibiotic
CC       nisin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Nisin exporter
CC       (TC 3.A.1.111.3) family. {ECO:0000305}.
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DR   EMBL; X68307; CAA48382.1; -; Genomic_DNA.
DR   EMBL; L16226; AAA25191.1; -; Genomic_DNA.
DR   EMBL; M65089; AAA73040.1; -; Genomic_DNA.
DR   PIR; E48951; E48951.
DR   PIR; S36736; S36736.
DR   RefSeq; WP_014570407.1; NZ_ML956318.1.
DR   AlphaFoldDB; Q03203; -.
DR   SMR; Q03203; -.
DR   TCDB; 3.A.1.111.3; 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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043213; P:bacteriocin transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; 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; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bacteriocin transport; Cell membrane; Membrane;
KW   Nucleotide-binding; Protein transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..600
FT                   /note="Nisin transport ATP-binding protein NisT"
FT                   /id="PRO_0000092632"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          34..317
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          352..592
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         386..393
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        14
FT                   /note="Y -> N (in Ref. 2; AAA25191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="E -> V (in Ref. 2; AAA25191)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   600 AA;  69210 MW;  AE92F317BD9045A5 CRC64;
     MDEVKEFTSK QFFYTLLTLP STLKLIFQLE KRYAIYLIVL NAITAFVPLA SLFIYQDLIN
     SVLGSGRHLI NIIIIYFIVQ VITTVLGQLE SYVSGKFDMR LSYSINMRLM RTTSSLELSD
     YEQADMYNII EKVTQDSTYK PFQLFNAIIV ELSSFISLLS SLFFIGTWNI GVAILLLIVP
     VLSLVLFLRV GQLEFLIQWQ RASSERETWY IVYLLTHDFS FKEIKLNNIS NYFIHKFGKL
     KKGFINQDLA IARKKTYFNI FLDFILNLIN ILTIFAMILS VRAGKLLIGN LVSLIQAISK
     INTYSQTMIQ NIYIIYNTSL FMEQLFEFLK RESVVHKKIE DTEICNQHIG TVKVINLSYV
     YPNSNAFALK NINLSFEKGE LTAIVGKNGS GKSTLVKIIS GLYQPTMGII QYDKMRSSLM
     PEEFYQKNIS VLFQDFVKYE LTIRENIGLS DLSSQWEDEK IIKVLDNLGL DFLKTNNQYV
     LDTQLGNWFQ EGHQLSGGQW QKIALARTFF KKASIYILDE PSAALDPVAE KEIFDYFVAL
     SENNISIFIS HSLNAARKAN KIVVMKDGQV EDVGSHDVLL RRCQYYQELY YSEQYEDNDE
 
 
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