TSSC1_PSEAE
ID TSSC1_PSEAE Reviewed; 498 AA.
AC Q9I748;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Type VI secretion system sheath protein TssC1 {ECO:0000303|PubMed:23341461};
DE AltName: Full=Sheath protein HsiC1;
GN Name=tssC1 {ECO:0000303|PubMed:23341461}; OrderedLocusNames=PA0084;
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, INTERACTION WITH TSSB1, DISRUPTION PHENOTYPE, AND DOMAIN.
RX PubMed=23341461; DOI=10.1074/jbc.m112.439273;
RA Lossi N.S., Manoli E., Foerster A., Dajani R., Pape T., Freemont P.,
RA Filloux A.;
RT "The HsiB1C1 (TssB-TssC) complex of the Pseudomonas aeruginosa type VI
RT secretion system forms a bacteriophage tail sheathlike structure.";
RL J. Biol. Chem. 288:7536-7548(2013).
RN [3]
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 [4] {ECO:0007744|PDB:5N8N}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.28 ANGSTROMS) OF 38-498, FUNCTION, AND
RP INTERACTION WITH TSSB1.
RX PubMed=29307484; DOI=10.1016/j.str.2017.12.005;
RA Salih O., He S., Planamente S., Stach L., MacDonald J.T., Manoli E.,
RA Scheres S.H.W., Filloux A., Freemont P.S.;
RT "Atomic Structure of Type VI Contractile Sheath from Pseudomonas
RT aeruginosa.";
RL Structure 26:329-336.E3(2018).
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. Forms the sheath of the structure by
CC assembling into tubules together with TssB1 resulting in the stacking
CC of cogwheel-like structures showing predominantly a 12-fold symmetry
CC (PubMed:23341461, PubMed:29307484). The sheath contracts to provide the
CC energy needed for effector delivery (PubMed:29307484).
CC {ECO:0000269|PubMed:23341461, ECO:0000269|PubMed:29307484}.
CC -!- SUBUNIT: Forms a heterodimer with TssB1. Heterodimers assemble to form
CC the sheat of the T6SS machinery (PubMed:23341461, PubMed:29307484).
CC Interacts with TssA1 (PubMed:27288401). {ECO:0000269|PubMed:23341461,
CC ECO:0000269|PubMed:27288401, ECO:0000269|PubMed:29307484}.
CC -!- DOMAIN: The C-terminal region is required for cogwheel and tubule
CC formation. {ECO:0000269|PubMed:23341461}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant shows a clear reduction in E.
CC coli killing and a lack of ability to secrete Hcp1, VgrG1a as well as
CC Tse3. {ECO:0000269|PubMed:23341461}.
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DR EMBL; AE004091; AAG03474.1; -; Genomic_DNA.
DR PIR; A83635; A83635.
DR RefSeq; NP_248774.1; NC_002516.2.
DR RefSeq; WP_003111626.1; NZ_QZGE01000015.1.
DR PDB; 5N8N; EM; 3.28 A; B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d=38-498.
DR PDBsum; 5N8N; -.
DR AlphaFoldDB; Q9I748; -.
DR SMR; Q9I748; -.
DR STRING; 287.DR97_3041; -.
DR PaxDb; Q9I748; -.
DR PRIDE; Q9I748; -.
DR EnsemblBacteria; AAG03474; AAG03474; PA0084.
DR GeneID; 879464; -.
DR KEGG; pae:PA0084; -.
DR PATRIC; fig|208964.12.peg.88; -.
DR PseudoCAP; PA0084; -.
DR HOGENOM; CLU_018386_1_0_6; -.
DR InParanoid; Q9I748; -.
DR OMA; EYGWCTS; -.
DR PhylomeDB; Q9I748; -.
DR BioCyc; PAER208964:G1FZ6-86-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR InterPro; IPR010269; T6SS_TssC-like.
DR InterPro; IPR044032; TssC1_C.
DR InterPro; IPR044031; TssC1_N.
DR PANTHER; PTHR35565; PTHR35565; 1.
DR Pfam; PF05943; VipB; 1.
DR Pfam; PF18945; VipB_2; 1.
DR TIGRFAMs; TIGR03355; VI_chp_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..498
FT /note="Type VI secretion system sheath protein TssC1"
FT /id="PRO_0000449263"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 173..188
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5N8N"
FT TURN 199..203
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 283..297
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:5N8N"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 339..347
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 379..387
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 391..411
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 450..459
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 467..475
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 481..488
FT /evidence="ECO:0007829|PDB:5N8N"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:5N8N"
SQ SEQUENCE 498 AA; 55772 MW; 49CFFB364D447D36 CRC64;
MAELSTENLA QGQTTTEQTS EFASLLLQEF KPKTERAREA VETAVRTLAE HALEQTSLIS
NDAIKSIESI IAALDAKLTA QVNLIMHHAD FQQLESAWRG LHYLVNNTET DEQLKIRVLN
ISKPELHKTL KKFKGTTWDQ SPIFKKLYEE EYGQFGGEPY GCLVGDYYFD QSPPDVELLG
EMAKISAAMH APFISAASPT VMGMGSWQEL SNPRDLTKIF TTPEYAGWRS LRESEDSRYI
GLTMPRFLAR LPYGAKTDPV EEFAFEEETD GADSSKYAWA NSAYAMAVNI NRSFKLYGWC
SRIRGVESGG EVQGLPAHTF PTDDGGVDMK CPTEIAISDR REAELAKNGF MPLLHKKNTD
FAAFIGAQSL QKPAEYDDPD ATANANLAAR LPYLFATCRF AHYLKCIVRD KIGSFKEKDE
MQRWLQDWIL NYVDGDPAHS TETTKAQHPL AAAEVVVEEV EGNPGYYNSK FFLRPHYQLE
GLTVSLRLVS KLPSAKEA
