VGR2B_PSEAE
ID VGR2B_PSEAE Reviewed; 1019 AA.
AC Q9I6M7;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Type VI secretion system spike protein VgrG2b {ECO:0000303|PubMed:31577948};
DE AltName: Full=Metallopeptidase effector VgrG2b {ECO:0000303|PubMed:31577948};
DE EC=3.4.24.- {ECO:0000269|PubMed:31577948};
GN Name=vgrG2b; OrderedLocusNames=PA0262;
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, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP HOST GCP1 AND GCP4.
RX PubMed=26037124; DOI=10.1128/mbio.00712-15;
RA Sana T.G., Baumann C., Merdes A., Soscia C., Rattei T., Hachani A.,
RA Jones C., Bennett K.L., Filloux A., Superti-Furga G., Voulhoux R.,
RA Bleves S.;
RT "Internalization of Pseudomonas aeruginosa Strain PAO1 into Epithelial
RT Cells Is Promoted by Interaction of a T6SS Effector with the Microtubule
RT Network.";
RL MBio 6:E00712-E00712(2015).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF HIS-935; GLU-936 AND
RP HIS-939, ACTIVE SITE, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=31577948; DOI=10.1016/j.celrep.2019.08.094;
RA Wood T.E., Howard S.A., Foerster A., Nolan L.M., Manoli E., Bullen N.P.,
RA Yau H.C.L., Hachani A., Hayward R.D., Whitney J.C., Vollmer W.,
RA Freemont P.S., Filloux A.;
RT "The Pseudomonas aeruginosa T6SS Delivers a Periplasmic Toxin that Disrupts
RT Bacterial Cell Morphology.";
RL Cell Rep. 29:187-201(2019).
RN [4]
RP FUNCTION, INTERACTION WITH TLA3, AND DISRUPTION PHENOTYPE.
RX PubMed=31231326; DOI=10.3389/fmicb.2019.01218;
RA Berni B., Soscia C., Djermoun S., Ize B., Bleves S.;
RT "A Type VI Secretion System Trans-Kingdom Effector Is Required for the
RT Delivery of a Novel Antibacterial Toxin in Pseudomonas aeruginosa.";
RL Front. Microbiol. 10:1218-1218(2019).
RN [5] {ECO:0007744|PDB:6H56}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 770-1019.
RA Wood T.E., Forster A., Manoli E., Howard S., Hachani A., Hayward A.D.,
RA Freemont P.S., Filloux A.;
RT "Effector domain of Pseudomonas aeruginosa VgrG2b.";
RL Submitted (JUL-2018) to the PDB data bank.
CC -!- FUNCTION: Part of the H2 type VI secretion system (H2-T6SS) specialized
CC secretion system, which delivers several virulence factors in both
CC prokaryotic and eukaryotic cells during infection (PubMed:26037124,
CC PubMed:31577948, PubMed:31231326). Forms the spike at the tip of the
CC elongating tube probably formed by haemolysin co-regulated protein
CC 2b/Hcp2b (Probable). Allows the delivery of the Tle3 antibacterial
CC toxin to target cells where it exerts its toxicity (PubMed:31231326).
CC Additionally, acts directly as an effector and promotes internalization
CC by interacting with the host gamma-tubulin ring complex
CC (PubMed:26037124). Elicits toxicity also in the bacterial periplasm and
CC disrupts bacterial cell morphology. Toxicity is counteracted by a
CC cognate immunity protein (PubMed:31577948).
CC {ECO:0000269|PubMed:26037124, ECO:0000269|PubMed:31231326,
CC ECO:0000269|PubMed:31577948, ECO:0000305|PubMed:31231326}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:31577948};
CC -!- SUBUNIT: Interacts with Tla3; this interaction promotes Tle3 loading
CC onto VgrG2b. Interacts with host gamma-tubulin ring complex components
CC GCP1 and GCP4. {ECO:0000269|PubMed:31231326}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26037124,
CC ECO:0000269|PubMed:31577948}. Note=Secreted by the H2 type VI (H2-T6SS)
CC secretion system involving VgrG2a into host cells upon infection.
CC {ECO:0000269|PubMed:26037124}.
CC -!- DOMAIN: The C-terminal region is part of a wide family of
CC metallopeptidase effectors. {ECO:0000269|PubMed:31577948}.
CC -!- DISRUPTION PHENOTYPE: Deletion leads to a 75% loss of internalization
CC of P.aeruginosa into host cell. {ECO:0000269|PubMed:26037124}.
CC -!- SIMILARITY: Belongs to the VgrG protein family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03651.1; -; Genomic_DNA.
DR PIR; A83613; A83613.
DR RefSeq; NP_248953.1; NC_002516.2.
DR RefSeq; WP_003147109.1; NZ_CP053028.1.
DR PDB; 6H56; X-ray; 3.20 A; A/B=770-1019.
DR PDBsum; 6H56; -.
DR AlphaFoldDB; Q9I6M7; -.
DR SMR; Q9I6M7; -.
DR STRING; 287.DR97_3224; -.
DR PaxDb; Q9I6M7; -.
DR EnsemblBacteria; AAG03651; AAG03651; PA0262.
DR GeneID; 881981; -.
DR KEGG; pae:PA0262; -.
DR PATRIC; fig|208964.12.peg.273; -.
DR PseudoCAP; PA0262; -.
DR HOGENOM; CLU_004121_1_4_6; -.
DR OMA; NADAQHN; -.
DR PhylomeDB; Q9I6M7; -.
DR BioCyc; PAER208964:G1FZ6-264-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033104; C:type VI protein secretion system complex; IGC:PseudoCAP.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033103; P:protein secretion by the type VI secretion system; IGC:PseudoCAP.
DR Gene3D; 2.40.50.230; -; 1.
DR InterPro; IPR006531; Gp5/Vgr_OB.
DR InterPro; IPR028244; T6SS_Rhs_Vgr_dom.
DR InterPro; IPR017847; T6SS_RhsGE_Vgr_subset.
DR InterPro; IPR006533; T6SS_Vgr_RhsGE.
DR InterPro; IPR037026; Vgr_OB-fold_dom_sf.
DR InterPro; IPR018769; VgrG2_C_DUF2345.
DR Pfam; PF10106; DUF2345; 1.
DR Pfam; PF04717; Phage_base_V; 1.
DR Pfam; PF13296; T6SS_Vgr; 1.
DR TIGRFAMs; TIGR01646; vgr_GE; 1.
DR TIGRFAMs; TIGR03361; VI_Rhs_Vgr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Secreted; Zinc.
FT CHAIN 1..1019
FT /note="Type VI secretion system spike protein VgrG2b"
FT /id="PRO_0000448915"
FT REGION 268..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 936
FT /evidence="ECO:0000269|PubMed:31577948,
FT ECO:0007744|PDB:6H56"
FT BINDING 935
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:31577948,
FT ECO:0007744|PDB:6H56"
FT BINDING 939
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:31577948,
FT ECO:0007744|PDB:6H56"
FT BINDING 983
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:31577948,
FT ECO:0007744|PDB:6H56"
FT MUTAGEN 935
FT /note="H->A: Abolishes bacterial periplasmic toxicity."
FT /evidence="ECO:0000269|PubMed:31577948"
FT MUTAGEN 936
FT /note="E->A: Abolishes bacterial periplasmic toxicity."
FT /evidence="ECO:0000269|PubMed:31577948"
FT MUTAGEN 939
FT /note="H->A: Abolishes bacterial periplasmic toxicity."
FT /evidence="ECO:0000269|PubMed:31577948"
FT HELIX 834..854
FT /evidence="ECO:0007829|PDB:6H56"
FT HELIX 868..878
FT /evidence="ECO:0007829|PDB:6H56"
FT TURN 884..886
FT /evidence="ECO:0007829|PDB:6H56"
FT STRAND 888..892
FT /evidence="ECO:0007829|PDB:6H56"
FT STRAND 906..912
FT /evidence="ECO:0007829|PDB:6H56"
FT HELIX 914..916
FT /evidence="ECO:0007829|PDB:6H56"
FT HELIX 922..924
FT /evidence="ECO:0007829|PDB:6H56"
FT HELIX 927..944
FT /evidence="ECO:0007829|PDB:6H56"
FT HELIX 949..962
FT /evidence="ECO:0007829|PDB:6H56"
FT HELIX 977..979
FT /evidence="ECO:0007829|PDB:6H56"
FT HELIX 982..998
FT /evidence="ECO:0007829|PDB:6H56"
FT HELIX 1000..1008
FT /evidence="ECO:0007829|PDB:6H56"
FT TURN 1009..1011
FT /evidence="ECO:0007829|PDB:6H56"
SQ SEQUENCE 1019 AA; 112964 MW; 51303C0019689C30 CRC64;
MRQRDLKFTF VVGEGKLAFD VVEFELEEAL CEPFRLNLKL ASDKNAIDFK QVLDQPGTFT
LWQDGRPARY VHGIVSHFTQ GSSGFRRTRY ELLLEPQLAR LELCCNWRIF QEKSVPEILQ
ALLKEHRVLD YEQRIYHEHL PREYCVQAGD SDHYLHDRLA FEEGLVYYFR FDEHRHTLVC
SDRLYVQERI AGGPVLFSAQ PEGDNPQPVL HSFRYSENVR TARQTQRDYS FKRPTYDQEH
HLAGEALEHQ GSSYERYDYP GRYKRSGAGR PFTESRLRGH RRDARVASVS GDDPRLIPGH
AFALEGHPRA DFNAWWRPVR VVHRGTQYAG QEEESADAPL GVSYDLRAEL VPEDVEWRPA
PLPRPRIDGP QIATVVGPAG EEIHCDEWGR VKVQFPWDRE GRHDEFSTCW IRVAQNWAGA
DWGHMAIPRI GQEVIVDYLD GDCDQPIVTG RTYRATNRPP YALPDHKILS TIKSKEYKGS
RANELRIDDT TAQISAALMS DHGASALHLG YLTHPRPEGG KPRGEGFELR TDEHGAVRAA
KGLLLSTEEQ LRAGAGHLDR GVVVQVLEAA LELARELGDY AGEHQGVGHD AAPQQTLQEA
VRDLGHGAND ESGKSNGGKP AIALSGPAGI AAATPASLTL AAGEHVDSVA RQNQQVTAGQ
KVVINAGSDI GLFAQGGELR QITHQGPMLL QAQKNDIRLE AKQSVEVSAS QQHVLVTAKE
HITLMCGGAY LTLKGGNIEL GMPGNFVVKA AKHSHVGAAS LEAELPQFEV GETQRRFVLK
QLDGQTAMPN VPYTITMANG EVIEGVTDAE GATQLLQKDA MNIAKVDMKH TKSPASAVAG
IAAAVGAAVA VGKLLGGPDA EAGRALSEGE ISLAKGVFGD SIDYSTVRLR DEDYVPWQGK
DYVMAPNGHI YFGEELRGVA DWSLESLQRQ GLFIHEMTHV WQHQHGVNVL LVGAYQQARQ
FLLGDQYAYR LEPGKTLKDY NIEQQGDIVR DYFLEKNEFG EASANSRFAG VLKNFPTGY
