FIMW_PSEAE
ID FIMW_PSEAE Reviewed; 607 AA.
AC Q9HUK7;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Cyclic-di-GMP receptor FimW {ECO:0000303|PubMed:30581112};
GN Name=fimW {ECO:0000303|PubMed:30581112};
GN OrderedLocusNames=PA4958 {ECO:0000312|EMBL:AAG08343.1};
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, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ARG-324; ARG-328; SER-437 AND GLY-440.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=30581112; DOI=10.1016/j.chom.2018.11.008;
RA Laventie B.J., Sangermani M., Estermann F., Manfredi P., Planes R., Hug I.,
RA Jaeger T., Meunier E., Broz P., Jenal U.;
RT "A surface-induced asymmetric program promotes tissue colonization by
RT Pseudomonas aeruginosa.";
RL Cell Host Microbe 25:140-152(2019).
CC -!- FUNCTION: High-affinity cyclic-di-GMP binding protein that regulates
CC type IV pili (T4P) elongation. Required for T4P-mediated surface
CC attachment and walking motility during the early phases of surface
CC colonization. Not required for twitching motility. Does not bind
CC related nucleotides such as GMP, GDP, GTP or ATP.
CC {ECO:0000269|PubMed:30581112}.
CC -!- SUBUNIT: Monomer in the absence of c-di-GMP. Forms dimers in the
CC presence of c-di-GMP. {ECO:0000269|PubMed:30581112}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Rapidly localizes to the cell
CC poles upon surface contact in a c-di-GMP-dependent manner. Dynamically
CC transitions between the cytoplasm and the cell poles, as a function of
CC c-di-GMP binding. {ECO:0000269|PubMed:30581112}.
CC -!- DOMAIN: Contains a PilZ-like fold that binds two molecules of c-di-GMP
CC via two well-conserved c-di-GMP-binding motifs, RXXXR and D/NXSXXG.
CC {ECO:0000269|PubMed:30581112}.
CC -!- DISRUPTION PHENOTYPE: Mutant has reduced surface piliation and is
CC unable to increase piliation upon surface exposure. It shows defects in
CC initial surface attachment and in early biofilm formation, but late
CC biofilm formation is not affected. Mutant loses walking motility but
CC twitching motility is barely affected. {ECO:0000269|PubMed:30581112}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG08343.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|PubMed:30581112};
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DR EMBL; AE004091; AAG08343.1; ALT_INIT; Genomic_DNA.
DR PIR; D83027; D83027.
DR RefSeq; NP_253645.1; NC_002516.2.
DR RefSeq; WP_003113922.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUK7; -.
DR STRING; 287.DR97_2311; -.
DR PaxDb; Q9HUK7; -.
DR PRIDE; Q9HUK7; -.
DR EnsemblBacteria; AAG08343; AAG08343; PA4958.
DR GeneID; 878415; -.
DR KEGG; pae:PA4958; -.
DR PATRIC; fig|208964.12.peg.5192; -.
DR PseudoCAP; PA4958; -.
DR HOGENOM; CLU_031627_1_0_6; -.
DR BioCyc; PAER208964:G1FZ6-5074-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW c-di-GMP; Cytoplasm; Nucleotide-binding; Reference proteome; Virulence.
FT CHAIN 1..607
FT /note="Cyclic-di-GMP receptor FimW"
FT /id="PRO_0000446520"
FT REGION 323..492
FT /note="PilZ-like domain"
FT /evidence="ECO:0000305|PubMed:30581112"
FT REGION 568..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 324..328
FT /note="RXXXR motif"
FT /evidence="ECO:0000305|PubMed:30581112"
FT MOTIF 435..440
FT /note="D/NXSXXG motif"
FT /evidence="ECO:0000305|PubMed:30581112"
FT MUTAGEN 324
FT /note="R->A: 5.6-fold decrease in c-di-GMP affinity."
FT /evidence="ECO:0000269|PubMed:30581112"
FT MUTAGEN 328
FT /note="R->A: Cannot bind c-di-GMP. Fails to localize to the
FT poles and to attach to the surface."
FT /evidence="ECO:0000269|PubMed:30581112"
FT MUTAGEN 437
FT /note="S->A: 9.3-fold decrease in c-di-GMP affinity."
FT /evidence="ECO:0000269|PubMed:30581112"
FT MUTAGEN 440
FT /note="G->A: Cannot bind c-di-GMP."
FT /evidence="ECO:0000269|PubMed:30581112"
SQ SEQUENCE 607 AA; 67829 MW; C1A1B553D1D66882 CRC64;
MENQSPHLSL RVPTPTQQNL SFCDATPKDI KYWLAHLPKA NLGETARQLY QGLIELNQLV
LPVEARLQLL ELFRPEVHFV CAHLERHFLN QAIVLDERPR KIANLCQALQ NHLAIGYKLI
VVQEAPRNSR DRAQLFAVGI QRAIRSLCGP LIRASQLYCP VPEGLWLELH QLYQLASQRG
VHRLAVRDEL AKHTPGLSVE QAYLIPLLLG CARCNQMRQN NIARLAEVLE PWSQLLSIQS
ATLPGSLFIA VPQIDGPPRY RSLYPETQLA SALGIDTQPL VELIREYLLQ PEAERAKARL
PLIEGVTLDL LQHLSSAWGD IAERTFQRTQ GQGQLTLCIG MSALHYFLAG RRPFNEVLQI
QEAPEAPRFK ADVQDAWAGA FDAQKVTDWQ PGMPLEEIEY RPHQSPRSVQ PGHPQAHAQA
DATEDYPTYA LPIVNHSPGG YCLSWPKEVP AQLQAGELVG LQDLPGQAWS IAVVRWIRQV
RNGGTQMGIE MIAPAAQPCG LQLLRKTEQS SHYLRALLLP AIAAISRPAT VITPRLPFQE
GSRVQINLHG EERRAVLNRR QASTGSFSQF EYRSAEPVNT PSDKPVTAPV ARPPAGEEDF
DSLWKSL
