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