FIML_PSEAE
ID FIML_PSEAE Reviewed; 562 AA.
AC Q9I2S3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Scaffold protein FimL {ECO:0000303|PubMed:27145134};
GN Name=fimL; OrderedLocusNames=PA1822;
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 [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 [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15720546; DOI=10.1111/j.1365-2958.2005.04479.x;
RA Whitchurch C.B., Beatson S.A., Comolli J.C., Jakobsen T., Sargent J.L.,
RA Bertrand J.J., West J., Klausen M., Waite L.L., Kang P.J.,
RA Tolker-Nielsen T., Mattick J.S., Engel J.N.;
RT "Pseudomonas aeruginosa fimL regulates multiple virulence functions by
RT intersecting with Vfr-modulated pathways.";
RL Mol. Microbiol. 55:1357-1378(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=21264306; DOI=10.1371/journal.pone.0015867;
RA Inclan Y.F., Huseby M.J., Engel J.N.;
RT "FimL regulates cAMP synthesis in Pseudomonas aeruginosa.";
RL PLoS ONE 6:e15867-e15867(2011).
RN [4]
RP FUNCTION, INTERACTION WITH PILG AND FIMV, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=27145134; DOI=10.1111/mmi.13410;
RA Inclan Y.F., Persat A., Greninger A., Von Dollen J., Johnson J., Krogan N.,
RA Gitai Z., Engel J.N.;
RT "A scaffold protein connects type IV pili with the Chp chemosensory system
RT to mediate activation of virulence signaling in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 101:590-605(2016).
CC -!- FUNCTION: Regulates multiple virulence functions including type IV
CC pilus (T4P)-mediated assembly and twitching motility as well as cAMP-
CC dependent virulence gene expression (PubMed:15720546). Regulates
CC intracellular cyclic AMP (cAMP) levels through the activation of
CC adenylate cyclase CyaB (PubMed:21264306). Functions also as a scaffold
CC linking FimV and PilG at the pole, where type IV pilus (T4P), the Chp
CC chemosensory system and the CyaB adenylate cyclase interact
CC (PubMed:27145134). {ECO:0000269|PubMed:15720546,
CC ECO:0000269|PubMed:21264306, ECO:0000269|PubMed:27145134}.
CC -!- SUBUNIT: Interacts with PilG and FimV. {ECO:0000269|PubMed:27145134}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27145134}.
CC Note=Localizes to poles in a FimV-dependent manner.
CC {ECO:0000269|PubMed:27145134}.
CC -!- DISRUPTION PHENOTYPE: Mutants show increased autolysis, reduced levels
CC of surface-assembled type IV pili, twitching motility and diminished
CC production of type III secreted effector. {ECO:0000269|PubMed:15720546,
CC ECO:0000269|PubMed:27145134}.
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DR EMBL; AE004091; AAG05211.1; -; Genomic_DNA.
DR PIR; H83418; H83418.
DR RefSeq; NP_250513.1; NC_002516.2.
DR RefSeq; WP_003098159.1; NZ_QZGE01000003.1.
DR AlphaFoldDB; Q9I2S3; -.
DR SMR; Q9I2S3; -.
DR STRING; 287.DR97_57; -.
DR PaxDb; Q9I2S3; -.
DR PRIDE; Q9I2S3; -.
DR EnsemblBacteria; AAG05211; AAG05211; PA1822.
DR GeneID; 881776; -.
DR KEGG; pae:PA1822; -.
DR PATRIC; fig|208964.12.peg.1892; -.
DR PseudoCAP; PA1822; -.
DR HOGENOM; CLU_017911_1_0_6; -.
DR InParanoid; Q9I2S3; -.
DR OMA; RLRHMYQ; -.
DR BioCyc; PAER208964:G1FZ6-1860-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004672; F:protein kinase activity; IEA:UniProt.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR InterPro; IPR036641; HPT_dom_sf.
DR SUPFAM; SSF47226; SSF47226; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..562
FT /note="Scaffold protein FimL"
FT /id="PRO_0000450453"
SQ SEQUENCE 562 AA; 60869 MW; 1824ADD203ADFA45 CRC64;
MVTGATSLSL VRDELFATME QAEQGLEQFI AERQNGSLLQ HAVECLQQIR GTLNLIELAG
AELLAQEALQ LATDIPTGVS EERDGQLAAL GNALYVLRRY LENVEANRQE IPELLLPAIN
EVRCAAGQPA LPESFFFSAR LDIPRPPSTA IDHLPSEAEL GEESRRMRHM YQIGLLGLIR
EQNLYPSLKL MGRALARLDS LHGGVARSRL CWIGAAAIES IVDGQLLPRK SRKQLFSRID
RELKQLLIGP AYEAPRHLLK ELLYLVALSD GQGPRSREVR ELHGLAPLPF TDHLLEEESQ
RLSGPGQSVM RSLSTAIREE LAGVKDMLDL IERGVAQPDS LTNLHAQLGK LSKTLGMVGL
NSAGTALQTQ LPTVAAWAAS GVADSPPALL RLADAVLYVE SMVGNLERGE RRIIRPTPAE
PGQEADAFAV HQLAEARIVV IEEAKAGLAL AKRAITAYLE SNGDKLNLAN VPASLQAVRG
GLWFLGQERA ALLVGGCADY IQQRMIETAQ MPSEQMLETL ADALTSLEYY LEGGAVLRPQ
GQPDVLDLAS ASVKALGLPV AA
