PILB_MYXXD
ID PILB_MYXXD Reviewed; 566 AA.
AC Q1D098;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Type IV pilus assembly ATPase PilB;
GN Name=pilB; OrderedLocusNames=MXAN_5788;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-327 AND GLU-391.
RX PubMed=18223089; DOI=10.1128/jb.01793-07;
RA Jakovljevic V., Leonardy S., Hoppert M., Soegaard-Andersen L.;
RT "PilB and PilT are ATPases acting antagonistically in type IV pilus
RT function in Myxococcus xanthus.";
RL J. Bacteriol. 190:2411-2421(2008).
RN [3]
RP FUNCTION, AND INTERACTION WITH PILC AND PILM.
RX PubMed=26851283; DOI=10.1074/jbc.m115.701284;
RA Bischof L.F., Friedrich C., Harms A., Soegaard-Andersen L.,
RA van der Does C.;
RT "The Type IV Pilus assembly ATPase PilB of Myxococcus xanthus interacts
RT with the inner membrane platform protein PilC and the nucleotide-binding
RT protein PilM.";
RL J. Biol. Chem. 291:6946-6957(2016).
RN [4]
RP FUNCTION, MUTAGENESIS OF MET-388, AND DISRUPTION PHENOTYPE.
RX PubMed=28779124; DOI=10.1038/s41598-017-07594-x;
RA Black W.P., Wang L., Jing X., Saldana R.C., Li F., Scharf B.E.,
RA Schubot F.D., Yang Z.;
RT "The type IV pilus assembly ATPase PilB functions as a signaling protein to
RT regulate exopolysaccharide production in Myxococcus xanthus.";
RL Sci. Rep. 7:7263-7263(2017).
RN [5] {ECO:0007744|PDB:3JC8}
RP STRUCTURE BY NMR, FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=26965631; DOI=10.1126/science.aad2001;
RA Chang Y.W., Rettberg L.A., Treuner-Lange A., Iwasa J., Sogaard-Andersen L.,
RA Jensen G.J.;
RT "Architecture of the type IVa pilus machine.";
RL Science 351:aad2001-aad2001(2016).
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. Acts as a molecular motor to provide the energy that is
CC required for biogenesis of the pilus and the extrusion of substrates
CC generated in the cytoplasm (PubMed:28779124, PubMed:26965631). PilB
CC ATPase activity is also essential for T4P extension while antagonist
CC PilT ATPase activity is required for T4P retraction (PubMed:18223089).
CC In addition, functions as a regulator of exopolysaccharide (EPS)
CC downstream of the T4P filament and upstream of the Dif signaling
CC (PubMed:28779124). {ECO:0000269|PubMed:18223089,
CC ECO:0000269|PubMed:26965631, ECO:0000269|PubMed:28779124}.
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts with PilC
CC (PubMed:26851283). Interacts with PilM (PubMed:26851283).
CC {ECO:0000250|UniProtKB:Q5SLC9, ECO:0000269|PubMed:26851283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18223089}.
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 -!- DISRUPTION PHENOTYPE: Deletion mutants show complete loss of T4P-
CC dependent motility since they did not assemble T4P (PubMed:18223089,
CC PubMed:28779124). PilB and PilT double mutant also lack T4P-dependent
CC motility (PubMed:26965631). {ECO:0000269|PubMed:18223089,
CC ECO:0000269|PubMed:26965631, ECO:0000269|PubMed:28779124}.
CC -!- SIMILARITY: Belongs to the GSP E family.
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DR EMBL; CP000113; ABF89788.1; -; Genomic_DNA.
DR RefSeq; WP_011555739.1; NC_008095.1.
DR PDB; 3JC8; EM; -; Ba/Bb/Bc/Bd/Be/Bf=1-566.
DR PDBsum; 3JC8; -.
DR AlphaFoldDB; Q1D098; -.
DR SMR; Q1D098; -.
DR STRING; 246197.MXAN_5788; -.
DR EnsemblBacteria; ABF89788; ABF89788; MXAN_5788.
DR GeneID; 41363031; -.
DR KEGG; mxa:MXAN_5788; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_1_7; -.
DR OMA; EINHGVD; -.
DR OrthoDB; 749544at2; -.
DR Proteomes; UP000002402; 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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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 3D-structure; ATP-binding; Cytoplasm; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..566
FT /note="Type IV pilus assembly ATPase PilB"
FT /id="PRO_0000450081"
FT BINDING 321..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22608"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q5SLC9"
FT MUTAGEN 327
FT /note="K->A: Strongly reduced ATPase activity."
FT /evidence="ECO:0000269|PubMed:18223089"
FT MUTAGEN 388
FT /note="M->I: Restored exopolysaccharide (EPS) production of
FT PilA mutant."
FT /evidence="ECO:0000269|PubMed:28779124"
FT MUTAGEN 391
FT /note="E->A: Strongly reduced ATPase activity."
FT /evidence="ECO:0000269|PubMed:18223089"
SQ SEQUENCE 566 AA; 62543 MW; 74FCB75DBF41EDF1 CRC64;
MSGRLGELLV RENLISVQQL RKAQEEQQKN GTRIGTALVK TGAIEESKLT DFLSKQYGVP
AINLKDFDVE PDIIKLVPKE VAEKHLVVPV NRAGPSLIVA MCDPSNIFAV DDLKFLTGYN
IETVVASEVS IREAIERYYA EKGPSLEDIV GDVGDDIEVT KEETENIDEM AKAADDAPVV
KLVNLILMDA IKKRASDIHV EPYEKDFRVR FRIDGVMYEV MRPPMKLRNA ITSRLKIMAS
LDISERRLPQ DGRIKIKMGG GKEMDFRVSV CPTLFGEKVV MRLLDKSNLQ LDMTKLGFDA
QPLAWFKEAI DRPYGMVLVT GPTGSGKTTT LYSALSSLNG LDTNICTAED PVEFNFAGIN
QVQMHDDIGL NFAAALRSFL RQDPDIIMIG EIRDFETAEI GVKAALTGHL VLSTLHTNDA
PGTVSRLLNM GIEPFLVTAS LNLILAQRLA RRLCPACKKP AENVDEQALI DAGVPPDKIG
TFTMYEKVGC RDCNDRGYRG RVAIYEVMPF WDGLKELVIN GASAAELKQE AIRLGMSSLR
MSGLRKMMDG ATTLEEVVGN TAPDRF
