GenomeNet

Database: UniProt
Entry: Q2JT92_SYNJA
LinkDB: Q2JT92_SYNJA
Original site: Q2JT92_SYNJA 
ID   Q2JT92_SYNJA            Unreviewed;       688 AA.
AC   Q2JT92;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Type IV pilus assembly protein PilB {ECO:0000313|EMBL:ABD00110.1};
GN   OrderedLocusNames=CYA_1965 {ECO:0000313|EMBL:ABD00110.1};
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321327 {ECO:0000313|EMBL:ABD00110.1, ECO:0000313|Proteomes:UP000008818};
RN   [1] {ECO:0000313|EMBL:ABD00110.1, ECO:0000313|Proteomes:UP000008818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab {ECO:0000313|EMBL:ABD00110.1,
RC   ECO:0000313|Proteomes:UP000008818};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
CC   -!- SIMILARITY: Belongs to the GSP E family.
CC       {ECO:0000256|ARBA:ARBA00006611}.
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; CP000239; ABD00110.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2JT92; -.
DR   STRING; 321327.CYA_1965; -.
DR   KEGG; cya:CYA_1965; -.
DR   eggNOG; COG2804; Bacteria.
DR   HOGENOM; CLU_013446_10_6_3; -.
DR   OrthoDB; 568371at2; -.
DR   Proteomes; UP000008818; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR007831; T2SS_GspE_N.
DR   PANTHER; PTHR30258:SF2; BACTERIOPHAGE ADSORPTION PROTEIN B; 1.
DR   PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR   Pfam; PF05157; MshEN; 1.
DR   Pfam; PF00437; T2SSE; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          382..517
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   688 AA;  76530 MW;  FD1606CADFDC1F2D CRC64;
     MSDLPSPPFT SRRAGAASKA LAIANVSITP FGRKLKELGF ADDKQIQDIQ NALKADREGG
     SKALALVVKE IVGKEITPDL ERAYKRQQLF ELKIIYGIPP LDIDLEPVEI SEMIGLIDSL
     LPLDICNRYK FLPIRRQDNQ VLVAMVRPDN LQALDDIQRR FRIQGLKLQR RVFTQRDFDA
     LINRYMDAQA ELLAIKGIND AAAPVQEEEE VVVNIAELDL DSIEDVAVDE AGEGSLEQQV
     KSADDAPIIK LSNQILVKAL QDGASDIHIE PQEEYLRIRF RKDGVLRQAF ENFPKKIVPA
     LTARFKIMSN LNIAERRLPQ DGRIRRVFKG RKVDFRVSTL PSRYGEKIVL RILDNSATQL
     GLDKLITDPE TLASFKEVVR RPFGLILVTG PTGSGKTTTL YSALAEVNDP GINISTAEDP
     IEYSLPGITQ VQVIREKGMD FAMILRAFLR QDPDVILVGE TRDHETAKTA IEASLTGHLV
     LTTLHTNDAP GAIARLTEMG IEPFMISSSL LGVLAQRLMR RVCTECRIPY HPTSEELARY
     GLSLSGDGEQ LTFYKANKLS PKEIEQRKAT GKPICEKCGG VGYKGRVGVY EFMRMNDRLA
     ELINKGAPTE VIKEAAVESG MKTLLAYSLM LVKQGLTTLE EVDRVILTDK GLETELKARA
     KALSTCRNCG AALQVDWMDC PYCLTPKF
//
DBGET integrated database retrieval system