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LCNCL_LACLA
ID   LCNCL_LACLA             Reviewed;         715 AA.
AC   Q9CJB8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Lactococcin transport/processing ATP-binding protein LcnC-like;
DE            EC=3.4.22.-;
DE            EC=7.-.-.-;
GN   Name=lcnC; OrderedLocusNames=LL0079; ORFNames=L82520;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Involved in the export process of a bacteriocin lactococcin.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. HlyB family.
CC       {ECO:0000305}.
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DR   EMBL; AE005176; AAK04177.1; -; Genomic_DNA.
DR   PIR; G86634; G86634.
DR   RefSeq; NP_266235.1; NC_002662.1.
DR   RefSeq; WP_010905094.1; NC_002662.1.
DR   AlphaFoldDB; Q9CJB8; -.
DR   SMR; Q9CJB8; -.
DR   STRING; 272623.L82520; -.
DR   MEROPS; C39.001; -.
DR   PaxDb; Q9CJB8; -.
DR   EnsemblBacteria; AAK04177; AAK04177; L82520.
DR   KEGG; lla:L82520; -.
DR   PATRIC; fig|272623.7.peg.88; -.
DR   eggNOG; COG2274; Bacteria.
DR   HOGENOM; CLU_000604_84_3_9; -.
DR   OMA; QQSHFIE; -.
DR   Proteomes; UP000002196; Chromosome.
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; Protease; Protein transport; Reference proteome;
KW   Thiol protease; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..715
FT                   /note="Lactococcin transport/processing ATP-binding protein
FT                   LcnC-like"
FT                   /id="PRO_0000092398"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          11..138
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   DOMAIN          168..450
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          482..715
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
FT   ACT_SITE        17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   BINDING         515..522
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   715 AA;  79865 MW;  360EBFEDFDBD8255 CRC64;
     MKFKKKNYTS QVDEMDCGCA ALSMILKSYG TEKSLASLRL LAGTTIEGTS ALGIKKAGEG
     LGFVVQVLRA DASLFEMKKV PYPFIAHVIK NQKYPHYYVI TGANKNSVFI ADPDPTVKMT
     KLSKEVFLSE WTGISLFLSP TPSYQPTKEK TSSLLSFIPI ITRQKKVILN IVIASFIVTL
     INILGSYYLQ SMIDSYIPNA LMGTLGIISV GLLLTYIIQQ VLEFAKAFLL NVLSQRLAID
     VILSYIRHIF QLPMSFFSTR RTGEITSRFS DASSILDAIA STILSLFLDL TIVLMTGLIL
     GLQNMQLFLL VLLAIPLYIV VIIIFTPLFE RQNHEVMQTN AILNSSIIED INGIETIKAL
     ASEQERYQKI DYEFASYLKE AFTLQQSEAI QTAIKTTVQL VLNVLILWFG ATLVMHQKIT
     LGQLITFNAL LSYFTNPITN IINLQTKLQK ARVANERLNE VYLVPSEFEE KKTELSLSHF
     NLNMSEISYQ YGFGRKVLSE IKLSIKENEK LTIVGISGSG KSTLVKLLVN FFQPTSGTIT
     LGGIDLQQFD KHQLRRLINY LPQQPYIFTG SIMDNLLLGA SEATSQEEII RAVELAEIRA
     DIEQMQLGYQ TELSSDASSL SGGQKQRIAL ARALLSPAKI LILDEATSNL DMITEKKILK
     NLLALDKTII FIAHRLSVAE MSHRIIVIEQ GKVIESGSHS ELLAQNGFYA QLYHN
 
 
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