ID   PILB_ACIAD              Reviewed;         579 AA.
AC   Q6FF45;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Type IV pilus assembly ATPase PilB {ECO:0000305};
GN   Name=pilB {ECO:0000303|PubMed:34145281};
GN   OrderedLocusNames=ACIAD0362 {ECO:0000312|EMBL:CAG67312.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [2]
RP   FUNCTION, OVEREXPRESSION, ACTIVITY REGULATION, INTERACTION WITH CPIA, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=34145281; DOI=10.1038/s41467-021-24124-6;
RA   Ellison C.K., Dalia T.N., Klancher C.A., Shaevitz J.W., Gitai Z.,
RA   Dalia A.B.;
RT   "Acinetobacter baylyi regulates type IV pilus synthesis by employing two
RT   extension motors and a motor protein inhibitor.";
RL   Nat. Commun. 12:3744-3744(2021).
CC   -!- FUNCTION: ATPase component of the type IV pilus (T4P) (By similarity).
CC       Acts as a molecular motor to provide the energy that is required for
CC       biogenesis of the pilus and the extrusion of substrates generated in
CC       the cytoplasm (By similarity). PilB is required for optimal T4P
CC       extension and, consequently, efficient natural transformation. May
CC       promote processive T4P extension (PubMed:34145281).
CC       {ECO:0000250|UniProtKB:P22608, ECO:0000269|PubMed:34145281}.
CC   -!- ACTIVITY REGULATION: Inhibited by the inhibitory protein CpiA.
CC       {ECO:0000269|PubMed:34145281}.
CC   -!- SUBUNIT: Interacts with CpiA. {ECO:0000269|PubMed:34145281}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22608}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene reduces transformation
CC       rates by two orders of magnitude. Natural transformation is
CC       undetectable in the pilB-tfpB double mutant. The pilB-tfpB-pilT triple
CC       mutant produces no detectable T4P fibers.
CC       {ECO:0000269|PubMed:34145281}.
CC   -!- MISCELLANEOUS: Both PilB and TfpB are essential for optimal T4P
CC       production, with each motor playing a distinct role in T4P extension.
CC       Overexpression of pilB does not restore the transformation defect of a
CC       tfpB mutant. {ECO:0000269|PubMed:34145281}.
CC   -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR   EMBL; CR543861; CAG67312.1; -; Genomic_DNA.
DR   SMR; Q6FF45; -.
DR   STRING; 62977.ACIAD0362; -.
DR   EnsemblBacteria; CAG67312; CAG67312; ACIAD0362.
DR   KEGG; aci:ACIAD0362; -.
DR   eggNOG; COG2804; Bacteria.
DR   HOGENOM; CLU_013446_10_1_6; -.
DR   OMA; NMGVPAF; -.
DR   Proteomes; UP000000430; 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; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009297; P:pilus assembly; IEA:InterPro.
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; Reference proteome; Zinc.
FT   CHAIN           1..579
FT                   /note="Type IV pilus assembly ATPase PilB"
FT                   /id="PRO_0000453801"
FT   BINDING         340..345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT   BINDING         470
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT   BINDING         473
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT   BINDING         507
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT   BINDING         510
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
SQ   SEQUENCE   579 AA;  64880 MW;  F28F45CFFE240018 CRC64;
     MISESQGGLM SAFTTPPKFS GFIRRLVEEG YVNAQNMQQA LEKAKKFKQD IVPYLIDNFS
     ISPLTIAEII SLEFGEPLLD LGVFDPALFL KDKIDEKLIQ KYRIMPLVHR GHVLYVATSN
     PTNIEAMDAI RFNSKLKVEP IIVEHDKLER LLSEHFVEET HFNFDTEELD LDVEVDPHTT
     DDDDEDDKLK DEAPIVKYIN KLLIDAIRMS ASDLHFEPYE KSYRVRYRVD GVLRLIATPP
     LQLATRLASR LKVMSQMDIS EKRVPQDGRI KLKMSKSKTI DFRVNSLPTL FGEKIVLRIL
     DPASAMLGID ALGYEPEQKA LFMEALNKPQ GMLLITGPTG SGKTVSLYTG LNILNTEHAN
     ISTAEDPVEI NLEGVNQVNV NPKVGLTFAA ALRSFLRQDP DIIMVGEIRD LETAEIAIKA
     AQTGHLVMST LHTNNAAETL TRLRNMGVAS FNIATSVNLV IAQRLARRLC SQCKRPIQVP
     ERSLLEMGFT PEDLAQPEFQ IFEPVGCHDC REGYKGRVGI YEVMKITPEI SKIIMEDGNA
     LEIAATAETL GFNNLRRSGL KKVMQGVTSL QEINRVTSE