PILB_THET8
ID PILB_THET8 Reviewed; 889 AA.
AC Q5SLC9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Type IV pilus assembly ATPase PilB;
GN Name=pilB; OrderedLocusNames=TTHA0364;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=29717025; DOI=10.1042/bcj20180167;
RA Sukmana A., Yang Z.;
RT "The type IV pilus assembly motor PilB is a robust hexameric ATPase with
RT complex kinetics.";
RL Biochem. J. 475:1979-1993(2018).
RN [3] {ECO:0007744|PDB:5IT5}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 505-889 IN COMPLEX WITH ATP AND
RP ZINC, FUNCTION, AND SUBUNIT.
RX PubMed=27667690; DOI=10.1016/j.str.2016.08.010;
RA Mancl J.M., Black W.P., Robinson H., Yang Z., Schubot F.D.;
RT "Crystal Structure of a Type IV Pilus Assembly ATPase: Insights into the
RT Molecular Mechanism of PilB from Thermus thermophilus.";
RL Structure 24:1886-1897(2016).
RN [4] {ECO:0007744|PDB:5OIU, ECO:0007744|PDB:6EJF, ECO:0007744|PDB:6F8L}
RP STRUCTURE BY ELECTRON MICROSCOPY (8.00 ANGSTROMS).
RX PubMed=30232337; DOI=10.1038/s41598-018-32218-3;
RA Collins R., Karuppiah V., Siebert C.A., Dajani R., Thistlethwaite A.,
RA Derrick J.P.;
RT "Structural cycle of the Thermus thermophilus PilF ATPase: the powering of
RT type IVa pilus assembly.";
RL Sci. Rep. 8:14022-14022(2018).
CC -!- FUNCTION: ATPase component of the type IV pilus (T4P) that plays a role
CC in surface and host cell adhesion, colonization, biofilm maturation,
CC virulence, and twitching, a form of surface-associated motility
CC facilitated by cycles of extension, adhesion, and retraction of T4P
CC fibers (By similarity) (PubMed:29717025). Acts as a molecular motor to
CC provide the energy that is required for biogenesis of the pilus and the
CC extrusion of substrates generated in the cytoplasm (PubMed:27667690).
CC PilB ATPase activity is also essential for T4P extension while
CC antagonist PilT ATPase activity is required for T4P retraction (By
CC similarity). {ECO:0000250|UniProtKB:P22608,
CC ECO:0000250|UniProtKB:Q1D098, ECO:0000269|PubMed:27667690,
CC ECO:0000269|PubMed:29717025}.
CC -!- SUBUNIT: Homohexamer (PubMed:29717025, PubMed:27667690). Interacts with
CC PilC (By similarity). {ECO:0000250|UniProtKB:P22608,
CC ECO:0000269|PubMed:27667690, ECO:0000269|PubMed:29717025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22608}.
CC Note=Displays polar localization. {ECO:0000250|UniProtKB:P22608}.
CC -!- DOMAIN: The ATP-binding site is essential for assembly of pili.
CC {ECO:0000250|UniProtKB:P22608}.
CC -!- SIMILARITY: Belongs to the GSP E family.
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DR EMBL; AP008226; BAD70187.1; -; Genomic_DNA.
DR RefSeq; WP_011173991.1; NC_006461.1.
DR RefSeq; YP_143630.1; NC_006461.1.
DR PDB; 5IT5; X-ray; 2.65 A; A/B/C/D/E/F=505-889.
DR PDB; 5OIU; X-ray; 2.44 A; A/B/C/D/E/F=500-889.
DR PDB; 6EJF; EM; 8.00 A; A/B/C/D/E/F=505-889, G/H/I/M/Q/R=330-475, J/K/L/N/O/P=163-299.
DR PDB; 6F8L; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-889.
DR PDBsum; 5IT5; -.
DR PDBsum; 5OIU; -.
DR PDBsum; 6EJF; -.
DR PDBsum; 6F8L; -.
DR AlphaFoldDB; Q5SLC9; -.
DR SMR; Q5SLC9; -.
DR STRING; 300852.55771746; -.
DR EnsemblBacteria; BAD70187; BAD70187; BAD70187.
DR GeneID; 3170115; -.
DR KEGG; ttj:TTHA0364; -.
DR PATRIC; fig|300852.9.peg.364; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_8_0_0; -.
DR OMA; LIRKPHG; -.
DR PhylomeDB; Q5SLC9; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.160; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR007831; T2SS_GspE_N.
DR Pfam; PF00437; T2SSE; 1.
DR Pfam; PF05157; T2SSE_N; 3.
DR SUPFAM; SSF160246; SSF160246; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..889
FT /note="Type IV pilus assembly ATPase PilB"
FT /id="PRO_0000450082"
FT BINDING 651..656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27667690,
FT ECO:0007744|PDB:5IT5"
FT BINDING 781
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27667690,
FT ECO:0007744|PDB:5IT5"
FT BINDING 784
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27667690,
FT ECO:0007744|PDB:5IT5"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27667690,
FT ECO:0007744|PDB:5IT5"
FT BINDING 819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27667690,
FT ECO:0007744|PDB:5IT5"
FT HELIX 506..521
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 524..530
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 532..541
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 544..552
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 556..566
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 578..586
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 589..600
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 603..611
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 627..637
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 640..647
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:5IT5"
FT HELIX 654..665
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 672..678
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 686..690
FT /evidence="ECO:0007829|PDB:5OIU"
FT TURN 693..696
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 699..706
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 722..734
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 737..742
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 748..756
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 761..767
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 768..780
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 782..788
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 792..797
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 802..805
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 810..813
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 817..819
FT /evidence="ECO:0007829|PDB:5OIU"
FT STRAND 822..835
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 838..845
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 850..859
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 865..873
FT /evidence="ECO:0007829|PDB:5OIU"
FT TURN 874..876
FT /evidence="ECO:0007829|PDB:5OIU"
FT HELIX 880..886
FT /evidence="ECO:0007829|PDB:5OIU"
SQ SEQUENCE 889 AA; 98213 MW; 35A4212C51646E20 CRC64;
MSVLTIGDKR LGAALLDAGL LTDEELQRAL ERHREVGGSL AEVLVDMGLL SERRIAQTIE
DRFGIPLVEL HRVEIPPKVK ALLPAEKAKE LKAIPFALDE EAGVVRVAFL NPLDTLSLEE
VEDLTGLVVE PYQTTKSAFL YALAKHYPEL GLPVPPPPSG EGQKDLKLGE LLLQKGWISR
EALEEALVEQ EKTGDLLGRI LVRKGLPEEA LYRALAEQKG LEFLESTEGI VPDPSAALLL
LRSDALRYGA VPIGFQNGEV EVVLSDPRHK EAVAQLLNRP ARFYLALPQA WEELFRRAYP
QKNRLGEVLV QEGKLSREAL KEALEVQKGL PRAKPLGEIL VELGLARPED VEEALQKQRR
GGGRLEDTLV QSGKLRPEAL AQAVATQLGY PYVDPEEDPP DPGAPLLLPE DLCRRYGVFP
HRLEGNRLVL LMKDPRNILA LDDVRLALKR KGLNYEVAPA VATEAAITKL IERFYGKAEL
SEIAKEFAKK QAEEEVPSPL ELDESAAQKF VKQVIREAFL QDASDIHIEP RQNDVQVRLR
IDGALRPYST LPKGALNAVI SVVKIMGGLN IAEKRLPQDG RVRYREGAID VDLRLSTLPT
VYGEKAVMRL LKKASDIPEI EDLGFAPGVF ERFKEVISKP YGIFLITGPT GSGKSFTTFS
ILKRIATPDK NTQTIEDPVE YEIPGINQTQ VNPQAGLTFA RALRAFLRQD PDIIMVGEIR
DSETAKIATE AALTGHLVIA TLHTNDAAQA ITRLDEMGVE PFNISAALIG VLSQRLVRRV
CEHCKVEVKP DPETLRRLGL SEAEIQGARL YKGMGCERCG GTGYKGRYAI HELLVVDDEI
RHAIVAGKSA TEIKEIARRK GMKTLREDGL YKALQGITTL EEVLARTIE
