PILS_PSEAE
ID PILS_PSEAE Reviewed; 530 AA.
AC P33639;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Sensor protein kinase PilS {ECO:0000303|PubMed:30042200};
DE EC=2.7.13.3 {ECO:0000269|PubMed:8550520};
GN Name=pilS; OrderedLocusNames=PA4546;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8097014; DOI=10.1111/j.1365-2958.1993.tb01158.x;
RA Hobbs M., Collie E.S.R., Free P.D., Livingston S.P., Mattick J.S.;
RT "PilS and PilR, a two-component transcriptional regulatory system
RT controlling expression of type 4 fimbriae in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 7:669-682(1993).
RN [2]
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 [3]
RP FUNCTION.
RC STRAIN=PAK;
RX PubMed=7911557; DOI=10.1007/bf00284205;
RA Boyd J.M., Koga T., Lory S.;
RT "Identification and characterization of PilS, an essential regulator of
RT pilin expression in Pseudomonas aeruginosa.";
RL Mol. Gen. Genet. 243:565-574(1994).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-319, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=PAK;
RX PubMed=8550520; DOI=10.1128/jb.178.3.831-839.1996;
RA Boyd J.M., Lory S.;
RT "Dual function of PilS during transcriptional activation of the Pseudomonas
RT aeruginosa pilin subunit gene.";
RL J. Bacteriol. 178:831-839(1996).
RN [5]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=PAK;
RX PubMed=10760172; DOI=10.1046/j.1365-2958.2000.01836.x;
RA Boyd J.M.;
RT "Localization of the histidine kinase PilS to the poles of Pseudomonas
RT aeruginosa and identification of a localization domain.";
RL Mol. Microbiol. 36:153-162(2000).
RN [6]
RP FUNCTION, INTERACTION WITH PILA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-24 AND ASN-323.
RX PubMed=27162347; DOI=10.1073/pnas.1512947113;
RA Kilmury S.L., Burrows L.L.;
RT "Type IV pilins regulate their own expression via direct intramembrane
RT interactions with the sensor kinase PilS.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:6017-6022(2016).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30042200; DOI=10.1128/mbio.01310-18;
RA Kilmury S.L.N., Burrows L.L.;
RT "The Pseudomonas aeruginosa PilSR Two-Component System Regulates Both
RT Twitching and Swimming Motilities.";
RL MBio 9:0-0(2018).
CC -!- FUNCTION: Member of the two-component regulatory system PilS/PilR that
CC regulates the expression of multiple genes including the type IV pilus
CC (T4P) major subunit PilA (PubMed:8097014, PubMed:7911557). Thereby,
CC plays a major role in the regulation of multiple motility pathways
CC (PubMed:30042200). Functions as a membrane-associated protein kinase
CC that phosphorylates PilR in response to environmental signals leading
CC to activation of specific gene promoters including the pilin gene
CC (PubMed:8550520, PubMed:27162347). {ECO:0000269|PubMed:27162347,
CC ECO:0000269|PubMed:30042200, ECO:0000269|PubMed:7911557,
CC ECO:0000269|PubMed:8097014, ECO:0000269|PubMed:8550520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:8550520};
CC -!- SUBUNIT: Interacts with PilA. {ECO:0000269|PubMed:27162347}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:27162347,
CC ECO:0000269|PubMed:8550520}; Multi-pass membrane protein {ECO:0000305}.
CC Note=Localizes at both poles of P.aeruginosa. Accumulates also at the
CC septum of dividing cells, so when the daughter cells separate, PilS is
CC already in place at both poles. {ECO:0000269|PubMed:10760172}.
CC -!- DOMAIN: The linker domain is the critical region for polar
CC localization. {ECO:0000269|PubMed:10760172}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant results in changes in swimming,
CC swarming and/or twitching motility associated with virulence in
CC specific hosts. {ECO:0000269|PubMed:30042200}.
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DR EMBL; Z12154; CAA78138.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07934.1; -; Genomic_DNA.
DR PIR; S33673; S33673.
DR RefSeq; NP_253236.1; NC_002516.2.
DR RefSeq; WP_003094692.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; P33639; -.
DR SMR; P33639; -.
DR STRING; 287.DR97_1850; -.
DR PaxDb; P33639; -.
DR PRIDE; P33639; -.
DR EnsemblBacteria; AAG07934; AAG07934; PA4546.
DR GeneID; 877621; -.
DR KEGG; pae:PA4546; -.
DR PATRIC; fig|208964.12.peg.4758; -.
DR PseudoCAP; PA4546; -.
DR HOGENOM; CLU_000445_114_39_6; -.
DR InParanoid; P33639; -.
DR OMA; ICRELCQ; -.
DR PhylomeDB; P33639; -.
DR BioCyc; PAER208964:G1FZ6-4639-MON; -.
DR BRENDA; 2.7.13.3; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0060491; P:regulation of cell projection assembly; IMP:PseudoCAP.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..530
FT /note="Sensor protein kinase PilS"
FT /id="PRO_0000074851"
FT TRANSMEM 25..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 196..260
FT /note="PAS"
FT DOMAIN 316..527
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 319
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MUTAGEN 24
FT /note="R->E: Complete loss of PilA autoregulation."
FT /evidence="ECO:0000269|PubMed:27162347"
FT MUTAGEN 319
FT /note="H->L: Loss of pilin gene expression."
FT /evidence="ECO:0000269|PubMed:8550520"
FT MUTAGEN 323
FT /note="N->A: Approximately threefold increase in basal pilA
FT transcription."
FT /evidence="ECO:0000269|PubMed:27162347"
SQ SEQUENCE 530 AA; 58985 MW; 1F6E0300E2E77A4C CRC64;
MRAERLRLSE EQGQRILRLY HLYRLTIGLV LVLLISSELE DQVLKLVHPE LFHVGSWCYL
VFNILVALFL PPSRQLLPIF ILALTDVLML CGLFYAGGGV PSGIGSLLVV AVAIANILLR
GRIGLVIAAA ASLGLLYLTF FLSLSSPDAT NHYVQAGGLG TLCFAAALVI QALVRRQEQT
ETLAEERAET VANLEELNAL ILQRMRTGIL VVDSRQAILL ANQAALGLLR QDDVQGASLG
RHSPMLMHCM KQWRLNPSLR PPTLKVVPDG PTVQPSFISL NREDDQHVLI FLEDISQIAQ
QAQQMKLAGL GRLTAGIAHE IRNPLGAISH AAQLLQESEE LDAPDRRLTQ IIQDQSKRMN
LVIENVLQLS RRRQAEPQQL DLKEWLQRFV DEYPGRLRND SQLHLQLGAG DIQTRMDPHQ
LNQVLSNLVQ NGLRYSAQAH GRGQVWLSLA RDPESDLPVL EVIDDGPGVP ADKLNNLFEP
FFTTESKGTG LGLYLSRELC ESNQARIDYR NREEGGGCFR ITFAHPRKLS
