TSSB1_PSEAE
ID TSSB1_PSEAE Reviewed; 172 AA.
AC Q9I749;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Type VI secretion system sheath protein TssB1 {ECO:0000303|PubMed:22906320};
DE AltName: Full=Sheath protein HsiB1;
GN Name=tssB1 {ECO:0000303|PubMed:22906320}; OrderedLocusNames=PA0083;
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 TAGJ, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK;
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 [3]
RP FUNCTION, AND INTERACTION WITH TSSC1.
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 [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] {ECO:0007744|PDB:4UQY, ECO:0007744|PDB:4UQZ}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), INTERACTION WITH TAGJ AND CLPV1,
RP AND FUNCTION.
RX PubMed=25305017; DOI=10.1074/jbc.m114.600510;
RA Foerster A., Planamente S., Manoli E., Lossi N.S., Freemont P.S.,
RA Filloux A.;
RT "Coevolution of the ATPase ClpV, the sheath proteins TssB and TssC, and the
RT accessory protein TagJ/HsiE1 distinguishes type VI secretion classes.";
RL J. Biol. Chem. 289:33032-33043(2014).
RN [6] {ECO:0007744|PDB:5N8N}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.28 ANGSTROMS) OF 4-135, FUNCTION, AND
RP INTERACTION WITH TSSC1.
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 TssC1 resulting in the stacking
CC of cogwheel-like structures showing predominantly a 12-fold symmetry
CC (PubMed:23341461, PubMed:25305017, PubMed:22906320). The sheath
CC contracts to provide the energy needed for effector delivery
CC (PubMed:29307484). {ECO:0000269|PubMed:22906320,
CC ECO:0000269|PubMed:23341461, ECO:0000269|PubMed:25305017,
CC ECO:0000269|PubMed:29307484}.
CC -!- SUBUNIT: Forms a heterodimer with TssC1. Heterodimers assemble to form
CC the sheath of the T6SS machinery (PubMed:29307484). Interacts with TagJ
CC (PubMed:22906320, PubMed:25305017). Interacts with TssA1
CC (PubMed:27288401). {ECO:0000269|PubMed:22906320,
CC ECO:0000269|PubMed:25305017, ECO:0000269|PubMed:27288401,
CC ECO:0000269|PubMed:29307484}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant shows a clear reduction in E.
CC coli killing. {ECO:0000269|PubMed:22906320}.
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; AAG03473.1; -; Genomic_DNA.
DR PIR; H83634; H83634.
DR RefSeq; NP_248773.1; NC_002516.2.
DR RefSeq; WP_003083666.1; NZ_QZGE01000015.1.
DR PDB; 4UQY; X-ray; 1.60 A; B=1-20.
DR PDB; 4UQZ; X-ray; 1.60 A; B=1-172.
DR PDB; 5N8N; EM; 3.28 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c=4-135.
DR PDBsum; 4UQY; -.
DR PDBsum; 4UQZ; -.
DR PDBsum; 5N8N; -.
DR AlphaFoldDB; Q9I749; -.
DR SMR; Q9I749; -.
DR STRING; 287.DR97_3040; -.
DR PaxDb; Q9I749; -.
DR PRIDE; Q9I749; -.
DR DNASU; 879476; -.
DR EnsemblBacteria; AAG03473; AAG03473; PA0083.
DR GeneID; 879476; -.
DR KEGG; pae:PA0083; -.
DR PATRIC; fig|208964.12.peg.87; -.
DR PseudoCAP; PA0083; -.
DR HOGENOM; CLU_111033_0_1_6; -.
DR InParanoid; Q9I749; -.
DR OMA; MTFESME; -.
DR PhylomeDB; Q9I749; -.
DR BioCyc; PAER208964:G1FZ6-85-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR InterPro; IPR008312; T6SS_TssB1.
DR PANTHER; PTHR35850; PTHR35850; 1.
DR Pfam; PF05591; T6SS_VipA; 1.
DR PIRSF; PIRSF028301; UCP028301; 1.
DR TIGRFAMs; TIGR03358; VI_chp_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..172
FT /note="Type VI secretion system sheath protein TssB1"
FT /id="PRO_0000449262"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4UQZ"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5N8N"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5N8N"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:5N8N"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:5N8N"
SQ SEQUENCE 172 AA; 18786 MW; 655C9C0B5C9D97F5 CRC64;
MGSTTSSQKF IARNRAPRVQ IEYDVELYGA EKKVQLPFVM GVMADLAGKP AEPQAAVADR
KFLEIDVDNF DARLKAMKPR VAFNVPNVLT GEGNLSLDIT FESMDDFSPA AVARKVDSLN
KLLEARTQLA NLLTYMDGKT GAEEMIMKAI KDPALLQALA SAPKPKDDEP QA
