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PILG_PSEAE
ID   PILG_PSEAE              Reviewed;         135 AA.
AC   P46384;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Protein PilG;
GN   Name=pilG; OrderedLocusNames=PA0408;
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].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=8104179; DOI=10.1128/jb.175.18.5934-5944.1993;
RA   Darzins A.;
RT   "The pilG gene product, required for Pseudomonas aeruginosa pilus
RT   production and twitching motility, is homologous to the enteric, single-
RT   domain response regulator CheY.";
RL   J. Bacteriol. 175:5934-5944(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, AND DISRUPTION PHENOTYPE.
RX   PubMed=20345659; DOI=10.1111/j.1365-2958.2010.07135.x;
RA   Fulcher N.B., Holliday P.M., Klem E., Cann M.J., Wolfgang M.C.;
RT   "The Pseudomonas aeruginosa Chp chemosensory system regulates intracellular
RT   cAMP levels by modulating adenylate cyclase activity.";
RL   Mol. Microbiol. 76:889-904(2010).
RN   [4]
RP   PHOSPHORYLATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27354279; DOI=10.1074/jbc.m116.737528;
RA   Silversmith R.E., Wang B., Fulcher N.B., Wolfgang M.C., Bourret R.B.;
RT   "Phosphoryl Group Flow within the Pseudomonas aeruginosa Pil-Chp
RT   Chemosensory System: DIFFERENTIAL FUNCTION OF THE EIGHT PHOSPHOTRANSFERASE
RT   AND THREE RECEIVER DOMAINS.";
RL   J. Biol. Chem. 291:17677-17691(2016).
RN   [5]
RP   FUNCTION.
RX   PubMed=28583947; DOI=10.1128/jb.00188-17;
RA   Buensuceso R.N.C., Daniel-Ivad M., Kilmury S.L.N., Leighton T.L.,
RA   Harvey H., Howell P.L., Burrows L.L.;
RT   "Cyclic AMP-Independent Control of Twitching Motility in Pseudomonas
RT   aeruginosa.";
RL   J. Bacteriol. 199:0-0(2017).
CC   -!- FUNCTION: Plays an essential role in both cAMP-dependent and
CC       independent regulation of twitching motility (PubMed:28583947).
CC       Regulates the cAMP-independent coordination of type IV pilus (T4P)
CC       biogenesis and retraction that plays a role in surface and host cell
CC       adhesion, colonization, biofilm maturation, virulence, and twitching
CC       (PubMed:20345659, PubMed:28583947). In addition, phosphorylated PilG is
CC       necessary for cAMP production via regulation of the adenylate cyclase
CC       CyaB. Acts therefore as a response regulator of the chemosensory
CC       system/Chp system (PubMed:20345659, PubMed:27354279).
CC       {ECO:0000269|PubMed:20345659, ECO:0000269|PubMed:27354279,
CC       ECO:0000269|PubMed:28583947}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:27354279}.
CC   -!- DISRUPTION PHENOTYPE: Deletion results in decreased cAMP, surface
CC       piliation, and twitching motility (PubMed:20345659, PubMed:27354279).
CC       Supplementation of pilG mutant with exogenous cAMP restores surface
CC       piliation but not twitching motility, suggesting that PilG regulates
CC       pilus biogenesis and function by at least two pathways
CC       (PubMed:20345659). {ECO:0000269|PubMed:20345659,
CC       ECO:0000269|PubMed:27354279}.
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DR   EMBL; L10831; AAA03067.1; -; Unassigned_DNA.
DR   EMBL; AE004091; AAG03797.1; -; Genomic_DNA.
DR   PIR; A48491; A48491.
DR   RefSeq; NP_249099.1; NC_002516.2.
DR   RefSeq; WP_003084583.1; NZ_QZGE01000016.1.
DR   AlphaFoldDB; P46384; -.
DR   SMR; P46384; -.
DR   STRING; 287.DR97_3376; -.
DR   PaxDb; P46384; -.
DR   PRIDE; P46384; -.
DR   DNASU; 878203; -.
DR   EnsemblBacteria; AAG03797; AAG03797; PA0408.
DR   GeneID; 878203; -.
DR   KEGG; pae:PA0408; -.
DR   PATRIC; fig|208964.12.peg.429; -.
DR   PseudoCAP; PA0408; -.
DR   HOGENOM; CLU_000445_69_17_6; -.
DR   InParanoid; P46384; -.
DR   OMA; IIFIDIM; -.
DR   PhylomeDB; P46384; -.
DR   BioCyc; PAER208964:G1FZ6-412-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Two-component regulatory system.
FT   CHAIN           1..135
FT                   /note="Protein PilG"
FT                   /id="PRO_0000081203"
FT   DOMAIN          9..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         58
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   135 AA;  14718 MW;  60CF6C38BC922E21 CRC64;
     MEQQSDGLKV MVIDDSKTIR RTAETLLKKV GCDVITAIDG FDALAKIADT HPNIIFVDIM
     MPRLDGYQTC ALIKNNSAFK STPVIMLSSK DGLFDKAKGR IVGSDQYLTK PFSKEELLGA
     IKAHVPSFTP VDAVS
 
 
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