ID   TFPB_ACIAD              Reviewed;         585 AA.
AC   Q6FA79;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Type IV pilus assembly ATPase TfpB {ECO:0000305};
DE   AltName: Full=Type four pilus PilB-like protein {ECO:0000303|PubMed:34145281};
GN   Name=tfpB {ECO:0000303|PubMed:34145281};
GN   OrderedLocusNames=ACIAD2241 {ECO:0000312|EMBL:CAG69034.1};
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, AND 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). TfpB is required for optimal T4P
CC       extension and, consequently, efficient natural transformation. May play
CC       a role in initiating T4P extension (PubMed:34145281).
CC       {ECO:0000250|UniProtKB:P22608, 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 tfpB-pilT mutant makes
CC       very few T4P. The pilB-tfpB-pilT triple mutant produces no detectable
CC       T4P fibers. {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 tfpB does not restore the transformation defect of a
CC       pilB mutant. {ECO:0000269|PubMed:34145281}.
CC   -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR   EMBL; CR543861; CAG69034.1; -; Genomic_DNA.
DR   RefSeq; WP_004927862.1; NC_005966.1.
DR   SMR; Q6FA79; -.
DR   STRING; 62977.ACIAD2241; -.
DR   EnsemblBacteria; CAG69034; CAG69034; ACIAD2241.
DR   GeneID; 45234570; -.
DR   KEGG; aci:ACIAD2241; -.
DR   eggNOG; COG2804; Bacteria.
DR   HOGENOM; CLU_013446_10_1_6; -.
DR   OMA; IVNIVDW; -.
DR   OrthoDB; 749544at2; -.
DR   BioCyc; ASP62977:ACIAD_RS10260-MON; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 1.
DR   SUPFAM; SSF160246; SSF160246; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00662; T2SP_E; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..585
FT                   /note="Type IV pilus assembly ATPase TfpB"
FT                   /id="PRO_0000453802"
FT   BINDING         346..351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT   BINDING         476
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT   BINDING         479
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT   BINDING         511
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT   BINDING         514
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SLC9"
SQ   SEQUENCE   585 AA;  66193 MW;  A84BA7E742AF7F41 CRC64;
     MTYHFEIDTQ WCLEQLLKDG RISERDKLLI QTTHRNKEQL KWHPLQWIAH FDLKDQAHTS
     KPFDILRLSQ WLAEKVGLPL YVIDPLKADV NMLTSVMSQE FALRNKILAV DVNPERILIG
     TDQPFVRDWV SNLELSLAPK KIELVLLSPD QLQRYLPEYY QVSRAVHSSK NATAYERDNK
     GVEALLQLGD NQNPDANDQH IVKLVDWILQ FAFEQGASDI HLEPRKEKGK VRFRIDGVLH
     TIYHMPANTL SAVIARIKIL GRLNVAEKRK PQDGRLKTRT PKGQETELRL STLPTAFGEK
     LVMRIFDPDV LVRSFEQLGF DEILLKQWQA LSRNSHGIIL VTGPTGSGKT TTLYSSLKQL
     ATDQVNVCTI EDPIEMLESS FNQMQVNAAI DLGFADGVRA LMRQDPDIIM VGEIRDQDTA
     NMAIQAALTG HLVLSTLHTN DAPSSLTRLH DLGVQPFLTA ATLLGVLAQR LVRQLCPHCK
     VLSDIDKQQW QHLTQDYEIA MPEQIYGPVG CDHCRQTGYK GRIGIYEFMS LDLNLKQLVS
     SEANLNQLKS EAKKQGIQPL RIAGARKILE GVTSLEEVLR VVPLT