PPRA_PSEAE
ID PPRA_PSEAE Reviewed; 922 AA.
AC Q9HWA7;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Two-component sensor PprA {ECO:0000303|PubMed:12499175};
DE EC=2.7.13.3 {ECO:0000305|PubMed:12499175};
GN Name=pprA {ECO:0000303|PubMed:12499175}; OrderedLocusNames=PA4293;
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, PHOSPHORYLATION, AND CATALYTIC ACTIVITY.
RC STRAIN=PAK;
RX PubMed=12499175; DOI=10.1128/aac.47.1.95-101.2003;
RA Wang Y., Ha U., Zeng L., Jin S.;
RT "Regulation of membrane permeability by a two-component regulatory system
RT in Pseudomonas aeruginosa.";
RL Antimicrob. Agents Chemother. 47:95-101(2003).
RN [3]
RP FUNCTION.
RX PubMed=23209420; DOI=10.1371/journal.ppat.1003052;
RA de Bentzmann S., Giraud C., Bernard C.S., Calderon V., Ewald F.,
RA Plesiat P., Nguyen C., Grunwald D., Attree I., Jeannot K., Fauvarque M.O.,
RA Bordi C.;
RT "Unique biofilm signature, drug susceptibility and decreased virulence in
RT Drosophila through the Pseudomonas aeruginosa two-component system PprAB.";
RL PLoS Pathog. 8:E1003052-E1003052(2012).
RN [4]
RP FUNCTION.
RX PubMed=21091863; DOI=10.1111/j.1462-2920.2010.02372.x;
RA Giraud C., Bernard C.S., Calderon V., Yang L., Filloux A., Molin S.,
RA Fichant G., Bordi C., de Bentzmann S.;
RT "The PprA-PprB two-component system activates CupE, the first non-
RT archetypal Pseudomonas aeruginosa chaperone-usher pathway system assembling
RT fimbriae.";
RL Environ. Microbiol. 13:666-683(2011).
RN [5]
RP FUNCTION, INDUCTION BY CARBON STARVATION, AND DISRUPTION PHENOTYPE.
RX PubMed=31492668; DOI=10.1128/aem.01705-19;
RA Wang C., Chen W., Xia A., Zhang R., Huang Y., Yang S., Ni L., Jin F.;
RT "Carbon starvation induces the expression of PprB-regulated genes in
RT Pseudomonas aeruginosa.";
RL Appl. Environ. Microbiol. 0:0-0(2019).
CC -!- FUNCTION: Member of the two-component regulatory system PprA/PprB
CC involved in biofilm formation by controlling the expression of many
CC related genes including type IVb pili major subunit flp pilin, adhesin
CC bapA or cupE fimbriae (PubMed:21091863, PubMed:23209420,
CC PubMed:31492668). Functions as a heme sensor histidine kinase which is
CC autophosphorylated at a histidine residue and transfers its phosphate
CC group to PprB (PubMed:12499175). {ECO:0000269|PubMed:12499175,
CC ECO:0000269|PubMed:21091863, ECO:0000269|PubMed:23209420,
CC ECO:0000269|PubMed:31492668}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:12499175};
CC -!- INDUCTION: By carbon starvation. This increased expression is
CC controlled by RpoS. {ECO:0000269|PubMed:31492668}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:12499175}.
CC -!- DISRUPTION PHENOTYPE: Mutant exhibits similar responses to carbon
CC starvation stress suggesting that PprB-mediated transcriptional
CC response is not transmitted through PprA.
CC {ECO:0000269|PubMed:31492668}.
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DR EMBL; AE004091; AAG07681.1; -; Genomic_DNA.
DR PIR; G83109; G83109.
DR RefSeq; NP_252983.1; NC_002516.2.
DR RefSeq; WP_003115766.1; NZ_QZGE01000034.1.
DR AlphaFoldDB; Q9HWA7; -.
DR STRING; 287.DR97_1468; -.
DR PaxDb; Q9HWA7; -.
DR PRIDE; Q9HWA7; -.
DR EnsemblBacteria; AAG07681; AAG07681; PA4293.
DR GeneID; 881624; -.
DR KEGG; pae:PA4293; -.
DR PATRIC; fig|208964.12.peg.4495; -.
DR PseudoCAP; PA4293; -.
DR HOGENOM; CLU_317582_0_0_6; -.
DR InParanoid; Q9HWA7; -.
DR OMA; QPLNVMR; -.
DR PhylomeDB; Q9HWA7; -.
DR BioCyc; PAER208964:G1FZ6-4377-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:PseudoCAP.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Two-component regulatory system.
FT CHAIN 1..922
FT /note="Two-component sensor PprA"
FT /id="PRO_0000448553"
FT DOMAIN 506..558
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 559..622
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 632..684
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 697..916
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 700
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 922 AA; 102118 MW; 26FEF57D640F84D6 CRC64;
MFEFSRSSSA EAERPEPFSQ EGPALWSASL RSWDLCFEMD EQDRVIRVGG RQAYRLQCAH
GLGEQPRPFA EYLERRAPGA PTLAGLRRGE RLDLTLRSDA AAPLTCRFQP MQPLDGLGRS
LLLGMDISDL NWQSDSQQHQ LQSLSLGKLI LSRLRHVSHG HLAEAVQEIL ESLSGAFQMQ
AIALLLGDGK GFCTVFASHV RPGSDSLLRP PLQLADDDLR EGAGARLLRR GEGASTLLRQ
IGEDALYLVP ATMRGGRLGA LLVRPMSLEQ LAQGPAPQDW QYLAELLANQ VADRCELHEQ
HDSSRKLGLL QEMIGGGWWR YWAEQELFEL APALHDSLGL TGEYRRVPLE HLQGLLQPAD
ADELGLRLRA SLRSGQALAQ DLCLRQPDSR GERRWLRIEG RPLGRGSALG LSGVLLDISE
GRRQEERAQA AHARLRSLID SAPVVIYVQR VEQGHLVPEF YSESASNLLG LDLQGQSWQA
LAERVHPDDL EAFFARGREL LREGRVKTRY RLADGQGNWH WLYDEAKLLR DAQGLPSEAV
GLWLDVTEQH LAAQRIAESE ERYRVLVEDS PALICRYTAD LVLTYVNRTF ADSLATSPER
LVGRRLDEWL AAEDASALRA RLLGSPREGA SEVPELRFNL PGQRFLWLVW AERPLFDARG
ELCEVQAVGR DNTPVRRAQQ QLAQGAKMAS LGEMVSGLAH EVKQPLHVLR MTLFNMRQRM
NSVGLDGDYL GEKLERMDAQ VLRVDRLVSH LGVFSRKSAL EALPFDPYAA FEGALGLLGE
GLRQHAIEVE CPAPTQRMVV RGQADQLEQV IINLLANARD ALLGNPGLAS RRVRLEQVAC
REPGWVELHV HDNGGGIEPL LLERIFEPFF TTKAEGKGTG LGLSVSHDLV RNMGGSLTAA
NQGEGALFVV RLPLAAPAEA GG
