GSPK_ECOLI
ID GSPK_ECOLI Reviewed; 327 AA.
AC P45762; Q2M6Z7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Putative type II secretion system protein K;
DE Short=T2SS protein K;
DE AltName: Full=Putative general secretion pathway protein K;
DE Flags: Precursor;
GN Name=gspK; Synonyms=yheJ; OrderedLocusNames=b3332, JW3294;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP LACK OF EXPRESSION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8655552; DOI=10.1128/jb.178.12.3544-3549.1996;
RA Francetic O., Pugsley A.P.;
RT "The cryptic general secretory pathway (gsp) operon of Escherichia coli K-
RT 12 encodes functional proteins.";
RL J. Bacteriol. 178:3544-3549(1996).
RN [4]
RP LACK OF EXPRESSION, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11118204; DOI=10.1093/emboj/19.24.6697;
RA Francetic O., Belin D., Badaut C., Pugsley A.P.;
RT "Expression of the endogenous type II secretion pathway in Escherichia coli
RT leads to chitinase secretion.";
RL EMBO J. 19:6697-6703(2000).
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 GspG. {ECO:0000250|UniProtKB:Q00518}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00518}.
CC -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC growth conditions. {ECO:0000269|PubMed:11118204}.
CC -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00518}.
CC -!- MISCELLANEOUS: Part of a cryptic operon that encodes proteins involved
CC in type II secretion machinery in other organisms, but is not expressed
CC in strain K12.
CC -!- SIMILARITY: Belongs to the GSP K family. {ECO:0000305}.
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DR EMBL; U18997; AAA58129.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76357.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77959.1; -; Genomic_DNA.
DR PIR; G65126; G65126.
DR RefSeq; NP_417791.1; NC_000913.3.
DR RefSeq; WP_001058522.1; NZ_STEB01000038.1.
DR AlphaFoldDB; P45762; -.
DR SMR; P45762; -.
DR BioGRID; 4263432; 343.
DR STRING; 511145.b3332; -.
DR PaxDb; P45762; -.
DR PRIDE; P45762; -.
DR EnsemblBacteria; AAC76357; AAC76357; b3332.
DR EnsemblBacteria; BAE77959; BAE77959; BAE77959.
DR GeneID; 947831; -.
DR KEGG; ecj:JW3294; -.
DR KEGG; eco:b3332; -.
DR PATRIC; fig|1411691.4.peg.3399; -.
DR EchoBASE; EB2731; -.
DR eggNOG; COG3156; Bacteria.
DR HOGENOM; CLU_057294_0_0_6; -.
DR InParanoid; P45762; -.
DR OMA; GWRNLND; -.
DR PhylomeDB; P45762; -.
DR BioCyc; EcoCyc:G7710-MON; -.
DR BioCyc; MetaCyc:G7710-MON; -.
DR PRO; PR:P45762; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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: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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..7
FT /note="Leader sequence"
FT /evidence="ECO:0000250|UniProtKB:Q00518"
FT /id="PRO_0000449555"
FT CHAIN 8..327
FT /note="Putative type II secretion system protein K"
FT /id="PRO_0000215007"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..327
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 327 AA; 37647 MW; 6AFD6A3D2DBF2123 CRC64;
MNNEQRGVAL LIVLMLLALM AALAADMTLS FHSQLQRTRQ VNHHLQRQYD IELAEKLALA
SLTQDVKDND RQTTLQQYWA QPQQLQLEDG NTVKWQLRDA QHCFNLNALA KISDDPLASP
DFPAQVFSAL LINAGIDRGN TDEIVQSIAD YIDVDDSPRF HGAEDSFYQS QTPPRHSANQ
MLFLTGELRQ IKGITENIYQ RLIPYVCVLP TTELSINLNM LTENDIPLFR ALFLNNITDA
DARVLLQKRP REGWLTTDAF LYWAQQDFSG VKPLVAQVKR HLFPYSRYFT LSTESISDEQ
SQGWQSHIFF NRKQQSAQIY RRTLQLY
