ID   TSSE1_PSEAE             Reviewed;         169 AA.
AC   Q9I745;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Type VI secretion system component TssE1 {ECO:0000303|PubMed:22906320};
GN   Name=tssE1 {ECO:0000303|PubMed:22906320}; OrderedLocusNames=PA0087;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-105.
RX   PubMed=21873404; DOI=10.1099/mic.0.051987-0;
RA   Lossi N.S., Dajani R., Freemont P., Filloux A.;
RT   "Structure-function analysis of HsiF, a gp25-like component of the type VI
RT   secretion system, in Pseudomonas aeruginosa.";
RL   Microbiology 157:3292-3305(2011).
RN   [3]
RP   INTERACTION WITH TSSB1, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22906320; DOI=10.1111/j.1365-2958.2012.08204.x;
RA   Lossi N.S., Manoli E., Simpson P., Jones C., Hui K., Dajani R.,
RA   Coulthurst S.J., Freemont P., Filloux A.;
RT   "The archetype Pseudomonas aeruginosa proteins TssB and TagJ form a novel
RT   subcomplex in the bacterial type VI secretion system.";
RL   Mol. Microbiol. 86:437-456(2012).
RN   [4]
RP   INTERACTION WITH TSSA1.
RX   PubMed=27288401; DOI=10.15252/embj.201694024;
RA   Planamente S., Salih O., Manoli E., Albesa-Jove D., Freemont P.S.,
RA   Filloux A.;
RT   "TssA forms a gp6-like ring attached to the type VI secretion sheath.";
RL   EMBO J. 35:1613-1627(2016).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=31379775; DOI=10.3389/fmicb.2019.01615;
RA   Liebl D., Robert-Genthon M., Job V., Cogoni V., Attree I.;
RT   "Baseplate component TssK and spatio-temporal assembly of T6SS in
RT   Pseudomonas aeruginosa.";
RL   Front. Microbiol. 10:1615-1615(2019).
CC   -!- FUNCTION: Core component of the H1 type VI (H1-T6SS) secretion system
CC       that plays a role in the release of toxins targeting both eukaryotic
CC       and prokaryotic species. Plays a role in correct elongation and
CC       stability of TssB1-sheath (PubMed:21873404, PubMed:22906320). Functions
CC       downstream of TssK1 and prevents detachment of TssB1-sheath and its
CC       premature disassembly. Once bound onto the sheath via an interaction
CC       with TssB1, provides an ideal docking point for ClpV1 to be recruited
CC       to the sheath (PubMed:31379775). {ECO:0000269|PubMed:21873404,
CC       ECO:0000269|PubMed:22906320, ECO:0000269|PubMed:31379775}.
CC   -!- SUBUNIT: Interacts with TssB1 (via N-terminus) (PubMed:22906320).
CC       Interacts with TssA1 (PubMed:27288401). {ECO:0000269|PubMed:22906320,
CC       ECO:0000269|PubMed:27288401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21873404}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant does not prevent TssB1 assembly
CC       into a sheath-like structure. However, the sheath exhibits an aberrant
CC       phenotype and break itself in smaller pieces.
CC       {ECO:0000269|PubMed:31379775}.
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; AE004091; AAG03477.1; -; Genomic_DNA.
DR   PIR; D83635; D83635.
DR   RefSeq; NP_248777.1; NC_002516.2.
DR   RefSeq; WP_003104971.1; NZ_QZGE01000015.1.
DR   AlphaFoldDB; Q9I745; -.
DR   STRING; 287.DR97_3044; -.
DR   PaxDb; Q9I745; -.
DR   DNASU; 879495; -.
DR   EnsemblBacteria; AAG03477; AAG03477; PA0087.
DR   GeneID; 879495; -.
DR   KEGG; pae:PA0087; -.
DR   PATRIC; fig|208964.12.peg.91; -.
DR   PseudoCAP; PA0087; -.
DR   HOGENOM; CLU_102944_0_0_6; -.
DR   InParanoid; Q9I745; -.
DR   OMA; DPYPLEF; -.
DR   PhylomeDB; Q9I745; -.
DR   BioCyc; PAER208964:G1FZ6-89-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007048; IraD/Gp25-like.
DR   InterPro; IPR017737; TssE1-like.
DR   Pfam; PF04965; GPW_gp25; 1.
DR   TIGRFAMs; TIGR03357; VI_zyme; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..169
FT                   /note="Type VI secretion system component TssE1"
FT                   /id="PRO_0000449264"
FT   MUTAGEN         105
FT                   /note="E->A: More than 90% loss of VgrG1a and VgrG1c
FT                   secretion."
FT                   /evidence="ECO:0000269|PubMed:21873404"
SQ   SEQUENCE   169 AA;  18693 MW;  15B3FBEA0AD07765 CRC64;
     MAELTLQERL QPSLLDRLTD DEPGNLKEAA ERRVLTLNQL KASVLRDLAW LFNTTSLFDH
     GPAARMPAGN SVLNYGLPAL AGHTASSVDV HAIEALLTET IATFEPRIIR SSLRVRAQLL
     PGEMDHNALS FEIEGDLWAE PAPLRLLLTT NLDLETGHVR VAQGERRRT