PILB_PSEAE
ID PILB_PSEAE Reviewed; 566 AA.
AC P22608; Q9HVQ0;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Type IV pilus assembly ATPase PilB;
GN Name=pilB; OrderedLocusNames=PA4526;
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 [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK;
RX PubMed=1971619; DOI=10.1128/jb.172.6.2911-2919.1990;
RA Nunn D., Bergman S., Lory S.;
RT "Products of three accessory genes, pilB, pilC, and pilD, are required for
RT biogenesis of Pseudomonas aeruginosa pili.";
RL J. Bacteriol. 172:2911-2919(1990).
RN [2]
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 [3]
RP MUTAGENESIS OF GLY-331, FUNCTION, AND DOMAIN.
RX PubMed=8102361; DOI=10.1128/jb.175.16.4962-4969.1993;
RA Turner L.R., Lara J.C., Nunn D.N., Lory S.;
RT "Mutations in the consensus ATP-binding sites of XcpR and PilB eliminate
RT extracellular protein secretion and pilus biogenesis in Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 175:4962-4969(1993).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15659660; DOI=10.1128/jb.187.3.829-839.2005;
RA Chiang P., Habash M., Burrows L.L.;
RT "Disparate subcellular localization patterns of Pseudomonas aeruginosa Type
RT IV pilus ATPases involved in twitching motility.";
RL J. Bacteriol. 187:829-839(2005).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLU-354; ASP-355; GLU-358; GLU-396; HIS-414
RP AND HIS-421.
RC STRAIN=PAK;
RX PubMed=18174131; DOI=10.1099/mic.0.2007/011320-0;
RA Chiang P., Sampaleanu L.M., Ayers M., Pahuta M., Howell P.L., Burrows L.L.;
RT "Functional role of conserved residues in the characteristic secretion
RT NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins
RT PilB, PilT and PilU.";
RL Microbiology 154:114-126(2008).
RN [6]
RP INTERACTION WITH PILC.
RX PubMed=23413032; DOI=10.1074/jbc.m113.453506;
RA Takhar H.K., Kemp K., Kim M., Howell P.L., Burrows L.L.;
RT "The platform protein is essential for type IV pilus biogenesis.";
RL J. Biol. Chem. 288:9721-9728(2013).
RN [7]
RP INTERACTION WITH FIMX, AND FUNCTION.
RX PubMed=28854278; DOI=10.1371/journal.ppat.1006594;
RA Jain R., Sliusarenko O., Kazmierczak B.I.;
RT "Interaction of the cyclic-di-GMP binding protein FimX and the Type 4 pilus
RT assembly ATPase promotes pilus assembly.";
RL PLoS Pathog. 13:e1006594-e1006594(2017).
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 (PubMed:15659660, PubMed:28854278). 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:8102361,
CC PubMed:18174131). PilB ATPase activity is also essential for T4P
CC extension while antagonist PilT ATPase activity is required for T4P
CC retraction (By similarity). {ECO:0000250|UniProtKB:Q1D098,
CC ECO:0000269|PubMed:15659660, ECO:0000269|PubMed:18174131,
CC ECO:0000269|PubMed:28854278, ECO:0000269|PubMed:8102361}.
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts with PilC
CC (PubMed:23413032). Interacts with FimX; this interaction positively
CC regulates T4P assembly and twitching motility by promoting the activity
CC of the PilB ATPase (PubMed:28854278). {ECO:0000250|UniProtKB:Q5SLC9,
CC ECO:0000269|PubMed:23413032, ECO:0000269|PubMed:28854278}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659660}.
CC Note=Displays polar localization. {ECO:0000269|PubMed:15659660}.
CC -!- DOMAIN: The ATP-binding site is essential for assembly of pili.
CC {ECO:0000269|PubMed:8102361}.
CC -!- DISRUPTION PHENOTYPE: Mutants fail to make pili although synthesize
CC wild-type levels of the pilin subunit PilA.
CC {ECO:0000269|PubMed:15659660}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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; M32066; AAA25732.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07914.1; -; Genomic_DNA.
DR PIR; A35384; A35384.
DR PIR; A83081; A83081.
DR RefSeq; NP_253216.1; NC_002516.2.
DR RefSeq; WP_003112841.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; P22608; -.
DR SMR; P22608; -.
DR STRING; 208964.PA4526; -.
DR TCDB; 3.A.15.2.1; the outer membrane protein secreting main terminal branch (mtb) family.
DR PaxDb; P22608; -.
DR PRIDE; P22608; -.
DR EnsemblBacteria; AAG07914; AAG07914; PA4526.
DR GeneID; 879459; -.
DR KEGG; pae:PA4526; -.
DR PATRIC; fig|208964.12.peg.4737; -.
DR PseudoCAP; PA4526; -.
DR HOGENOM; CLU_013446_10_1_6; -.
DR InParanoid; P22608; -.
DR OMA; NMGVPAF; -.
DR PhylomeDB; P22608; -.
DR BioCyc; PAER208964:G1FZ6-4616-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PseudoCAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048870; P:cell motility; IMP:CACAO.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043683; P:type IV pilus assembly; IDA:PseudoCAP.
DR GO; GO:0043107; P:type IV pilus-dependent motility; IDA:PseudoCAP.
DR Gene3D; 3.30.300.160; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR013374; ATPase_typ4_pilus-assembl_PilB.
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; 1.
DR SUPFAM; SSF160246; SSF160246; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02538; type_IV_pilB; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Fimbrium biogenesis; Metal-binding;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..566
FT /note="Type IV pilus assembly ATPase PilB"
FT /id="PRO_0000207294"
FT BINDING 326..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:8102361"
FT BINDING 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT BINDING 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT BINDING 494
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT VARIANT 26
FT /note="V -> L (in strain: PAK)"
FT VARIANT 30
FT /note="A -> T (in strain: PAK)"
FT VARIANT 46
FT /note="S -> N (in strain: PAK)"
FT VARIANT 74
FT /note="K -> R (in strain: PAK)"
FT VARIANT 109
FT /note="P -> A (in strain: PAK)"
FT VARIANT 146
FT /note="S -> N (in strain: PAK)"
FT VARIANT 164..171
FT /note="IGSADKST -> VGVKETSG (in strain: PAK)"
FT VARIANT 175..176
FT /note="AS -> TG (in strain: PAK)"
FT VARIANT 467
FT /note="E -> D (in strain: PAK)"
FT VARIANT 470
FT /note="R -> K (in strain: PAK)"
FT VARIANT 481..482
FT /note="DK -> EL (in strain: PAK)"
FT MUTAGEN 331
FT /note="G->S: Complete loss of pili formation."
FT /evidence="ECO:0000269|PubMed:8102361"
FT MUTAGEN 354
FT /note="E->Q: About 70% reduced twitching motility."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 355
FT /note="D->N: No loss of twitching motility."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 358
FT /note="E->Q: Loss of twitching motility."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 396
FT /note="E->Q: Loss of twitching motility."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 414
FT /note="H->A: Loss of twitching motility."
FT /evidence="ECO:0000269|PubMed:18174131"
FT MUTAGEN 421
FT /note="H->A: Loss of twitching motility."
FT /evidence="ECO:0000269|PubMed:18174131"
SQ SEQUENCE 566 AA; 62328 MW; B51F5147AA0FECB5 CRC64;
MNDSIQLSGL SRQLVQANLL DEKTAVQAQA QAQRNKLSLV THLVQSKLVS GLALAELSAE
QFGIAYCDLN SLDKESFPRD AISEKLVRQH RVIPLWRRGN KLFVGISDPA NHQAINDVQF
STGLTTEAIL VEDDKLGLAI DKLFESATDG LAGLDDVDLE GLDIGSADKS TQEDASAEAD
DAPVVRFVNK MLLDAIKGGS SDLHFEPYEK IYRVRFRTDG MLHEVAKPPI QLASRISARL
KVMAGLDISE RRKPQDGRIK MRVSKTKSID FRVNTLPTLW GEKIVMRILD SSSAQMGIDA
LGYEEDQKEL YLAALKQPQG MILVTGPTGS GKTVSLYTGL NILNTTDINI STAEDPVEIN
LEGINQVNVN PRQGMDFSQA LRAFLRQDPD VIMVGEIRDL ETAEIAIKAA QTGHMVMSTL
HTNSAAETLT RLLNMGVPAF NLATSVNLII AQRLARKLCS HCKKEHEVPR ETLLHEGFPE
DKIGTFKLYS PVGCDHCKNG YKGRVGIYEV VKNTPALQRI IMEEGNSIEI AEQARKEGFN
DLRTSGLLKA MQGITSLEEV NRVTKD
