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GSPK_PECCC
ID   GSPK_PECCC              Reviewed;         328 AA.
AC   P31706;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Type II secretion system protein K;
DE            Short=T2SS protein K;
DE   AltName: Full=General secretion pathway protein K;
DE   AltName: Full=Pectic enzymes secretion protein OutK;
DE   Flags: Precursor;
GN   Name=outK;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA   Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA   Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA   Salmond G.P.C.;
RT   "Molecular cloning and characterization of 13 out genes from Erwinia
RT   carotovora subspecies carotovora: genes encoding members of a general
RT   secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL   Mol. Microbiol. 8:443-456(1993).
CC   -!- FUNCTION: Component of the type II secretion system required for the
CC       energy-dependent secretion of extracellular factors such as proteases
CC       and toxins from the periplasm. Plays a role in pseudopilus assembly and
CC       seems to control its length. Interacts with the pseudopilus tip complex
CC       that is critical for the recognition and binding of secretion
CC       substrates. {ECO:0000250|UniProtKB:Q00518}.
CC   -!- SUBUNIT: Type II secretion is composed of four main components: the
CC       outer membrane complex, the inner membrane complex, the cytoplasmic
CC       secretion ATPase and the periplasm-spanning pseudopilus. Interacts with
CC       core component OutG. {ECO:0000250|UniProtKB:Q00518}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q00518}.
CC   -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00518}.
CC   -!- SIMILARITY: Belongs to the GSP K family. {ECO:0000305}.
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DR   EMBL; X70049; CAA49652.1; -; Genomic_DNA.
DR   PIR; S32865; S32865.
DR   AlphaFoldDB; P31706; -.
DR   SMR; P31706; -.
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:0009306; P:protein secretion; IEA:InterPro.
DR   Gene3D; 1.10.40.60; -; 2.
DR   InterPro; IPR005628; GspK.
DR   InterPro; IPR038072; GspK_central_sf.
DR   InterPro; IPR045584; Pilin-like.
DR   PANTHER; PTHR38831; PTHR38831; 1.
DR   Pfam; PF03934; T2SSK; 1.
DR   PIRSF; PIRSF002786; XcpX; 1.
DR   SUPFAM; SSF158544; SSF158544; 2.
DR   SUPFAM; SSF54523; SSF54523; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..7
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000250|UniProtKB:Q00518"
FT                   /id="PRO_0000449556"
FT   CHAIN           8..328
FT                   /note="Type II secretion system protein K"
FT                   /id="PRO_0000449557"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..328
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   328 AA;  36570 MW;  CDC2ECD3576838DB CRC64;
     MRSRQRGAAL LVVLLILALM VTIAAVITER TGKAFLRTES HLSRQQAKWY ALGAETLSGQ
     ILQRDARNMP GRTFAGQNWS QPGLRFPVDG GEITGQISDA RTCFNVNAIN QGVDNESTLV
     KTPYPAQVFR LLLKNLGEET DRAEKITAAV RDWIDADNYP SANGAEDDVY AALPVPYRTA
     NQRMSEISEL RSVYGIDSDL YRRLLPYVCA LPVDAMSINI NTLTEFDAPL LSAVFLNEMT
     MSQAKALVQQ RPRMGWASLE VLQQTGLLPP NSKNTAQRVL AVKSEWFFVK LQVRVGDSDF
     HQRSLLHLSG QKVQVVQRQY GGYRTVNP
 
 
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