ID GSPE_ECOLI Reviewed; 493 AA.
AC P45759; Q2M6Z1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Putative type II secretion system protein E;
DE Short=T2SS protein E;
DE EC=7.4.2.8 {ECO:0000250|UniProtKB:P37093};
DE AltName: Full=Putative general secretion pathway protein E;
DE AltName: Full=Type II traffic warden ATPase;
GN Name=gspE; Synonyms=yheG; OrderedLocusNames=b3326, JW3288;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; 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: ATPase component of the type II secretion system required for
CC the energy-dependent secretion of extracellular factors such as
CC proteases and toxins from the periplasm. Acts as a molecular motor to
CC provide the energy that is required for assembly of the pseudopilus and
CC the extrusion of substrates generated in the cytoplasm.
CC {ECO:0000250|UniProtKB:Q00512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000250|UniProtKB:P37093};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P37093};
CC -!- SUBUNIT: Forms homooligomers; most probably hexamers (By similarity).
CC Interacts with GspL (By similarity). {ECO:0000250|UniProtKB:P37093,
CC ECO:0000250|UniProtKB:Q00512}.
CC -!- INTERACTION:
CC P45759; P60422: rplB; NbExp=2; IntAct=EBI-1132437, EBI-543515;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00512}. Note=Membrane association is not an
CC intrinsic property but requires the GspL gene product.
CC {ECO:0000250|UniProtKB:Q00512}.
CC -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC growth conditions. {ECO:0000269|PubMed:11118204}.
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 E family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U18997; AAA58123.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76351.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77965.1; -; Genomic_DNA.
DR PIR; A65126; A65126.
DR RefSeq; NP_417785.1; NC_000913.3.
DR RefSeq; WP_001219894.1; NZ_SSZK01000040.1.
DR AlphaFoldDB; P45759; -.
DR SMR; P45759; -.
DR BioGRID; 4261298; 330.
DR BioGRID; 852135; 1.
DR IntAct; P45759; 1.
DR STRING; 511145.b3326; -.
DR PaxDb; 511145-b3326; -.
DR EnsemblBacteria; AAC76351; AAC76351; b3326.
DR GeneID; 947823; -.
DR KEGG; ecj:JW3288; -.
DR KEGG; eco:b3326; -.
DR PATRIC; fig|1411691.4.peg.3405; -.
DR EchoBASE; EB2728; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_3_6; -.
DR InParanoid; P45759; -.
DR OMA; RFRVRYK; -.
DR OrthoDB; 9804785at2; -.
DR PhylomeDB; P45759; -.
DR BioCyc; EcoCyc:G7704-MONOMER; -.
DR BioCyc; MetaCyc:G7704-MONOMER; -.
DR PRO; PR:P45759; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015627; C:type II protein secretion system complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
DR CDD; cd01129; PulE-GspE-like; 1.
DR Gene3D; 3.30.450.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.300.160; Type II secretion system, protein E, N-terminal domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS_dom.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR013369; T2SS_GspE.
DR NCBIfam; TIGR02533; type_II_gspE; 1.
DR PANTHER; PTHR30258:SF27; TYPE II SECRETION SYSTEM PROTEIN E-RELATED; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane; Metal-binding;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Transport; Zinc.
FT CHAIN 1..493
FT /note="Putative type II secretion system protein E"
FT /id="PRO_0000207284"
FT BINDING 249..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P37093"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P37093"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P37093"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P37093"
SQ SEQUENCE 493 AA; 54611 MW; A13C67C3D48596CA CRC64;
MRIHSPYPAS WALAQRIGYL YSEGEIIYLA DTPFERLLDI QRQVGQCQTM TSLSQADFEA
RLEAVFHQNT GESQQIAQDI DQSVDLLSLS EEMPANEDLL NEDSAAPVIR LINAILSEAI
KETASDIHIE TYEKTMSIRF RIDGVLRTIL QPNKKLAALL ISRIKVMARL DIAEKRIPQD
GRISLRIGRR NIDVRVSTLP SIYGERAVLR LLDKNSLQLS LNNLGMTAAD KQDLENLIQL
PHGIILVTGP TGSGKSTTLY AILSALNTPG RNILTVEDPV EYELEGIGQT QVNTRVDMSF
ARGLRAILRQ DPDVVMVGEI RDTETAQIAV QASLTGHLVL STLHTNSASG AVTRLRDMGV
ESFLLSSSLA GIIAQRLVRR LCPQCRQFTP VSPQQAQMFK YHQLAVTTIG TPVGCPHCHQ
SGYQGRMAIH EMMVVTPELR AAIHENVDEQ ALERLVRQQH KALIKNGLQK VISGDTSWDE
VMRVASATLE SEA
//
