ARUS_PSEAE
ID ARUS_PSEAE Reviewed; 998 AA.
AC Q9HUI3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Sensor histidine kinase AruS;
DE EC=2.7.13.3;
GN Name=aruS; OrderedLocusNames=PA4982;
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, PATHWAY, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=17416670; DOI=10.1128/jb.00261-07;
RA Yang Z., Lu C.D.;
RT "Functional genomics enables identification of genes of the arginine
RT transaminase pathway in Pseudomonas aeruginosa.";
RL J. Bacteriol. 189:3945-3953(2007).
CC -!- FUNCTION: Member of the two-component regulatory system AruS/AruR,
CC which is involved in the regulation of the arginine transaminase (ATA)
CC pathway in response to exogeneous L-arginine. Probably functions as a
CC sensor kinase that phosphorylates AruR. {ECO:0000269|PubMed:17416670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation [regulation].
CC {ECO:0000269|PubMed:17416670}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Autophosphorylated. Activation may require a sequential transfer
CC of a phosphate group from a His in the primary transmitter domain, to
CC an Asp in the receiver domain and to a His in the secondary transmitter
CC domain (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Disruption in the aruF mutant prevents growth on
CC L-arginine. {ECO:0000269|PubMed:17416670}.
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DR EMBL; AE004091; AAG08367.1; -; Genomic_DNA.
DR PIR; G83022; G83022.
DR AlphaFoldDB; Q9HUI3; -.
DR SMR; Q9HUI3; -.
DR STRING; 287.DR97_2335; -.
DR PaxDb; Q9HUI3; -.
DR PRIDE; Q9HUI3; -.
DR EnsemblBacteria; AAG08367; AAG08367; PA4982.
DR PseudoCAP; PA4982; -.
DR HOGENOM; CLU_000445_104_15_6; -.
DR InParanoid; Q9HUI3; -.
DR OMA; YRREMRD; -.
DR PhylomeDB; Q9HUI3; -.
DR UniPathway; UPA00073; -.
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:0006527; P:arginine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR033414; Sensor_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF17149; CHASE5; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..998
FT /note="Sensor histidine kinase AruS"
FT /id="PRO_0000418389"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 417..473
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 513..734
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 751..869
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 894..987
FT /note="HPt"
FT REGION 27..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..179
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 516
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 800
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 933
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 998 AA; 109138 MW; 6372AA8E44A6E9B4 CRC64;
MAAGRPGTGC GDHPLLRLSG IPADFLERRP AGPGAGAGAG EAAVRRAGLP GRGGGAGQLA
ALPARRRRRT GRPDTGLPHA RARSRPGVFR RAGAARGGGD LLQPPAAGAH PIPRRPRRLS
RRAVVRRKLR GGLRPLRRPP RQRRMGFRQP TELRQAGAPA HRLHRPRTTH RHAVRRAPGR
RREHPCAART ADGGLPAGGG LAALAAGGED GRDRPGPAWL SRRRQHPALA GRQRARLSAP
RRQPRGRLVS GHGGVLARRL LWRVLLFSLC FTVLAGAVQL FFEYRREMRE IEARLELIRS
GYLASFERSL WDLNQEQLNV QLRGLGDFPD IARVSLQSAD FNLLQGDQRP RGMLRVERFP
LSYQPPGGER RQLGELEIAI DLAAVYRRLV SGGLASLLWM GSFLCGLAVA LSWLFHSLVT
RHLWRMSEFA GHIAEGDLQQ PLRLDKVDRE RDEIDAVAAA LEDMRQALRT DRRRRDADRD
ELRRQVERRT ASLRRAKDQA EAADRAKSRF LATMSHEIRT PLNGILGMAE LLREASLGER
DRQRLRALAT AGEGLLAILN EVLHFARLEE APDVPEAVDF SLRSLLEDVL TLLEPRAREN
ATRLDLWLDP QVHDGHRGAE QFLRQVLTNL LGNAVKFTEA GEVRVRVERL ARSAGSERLR
LSVADDGIGI PEEMRERIFE RFTQGGDAVT RRYGGTGLGL AISKRLVEAL GGRIGVESRV
GQGSTFWFEI ELALASLSGA TPPAASVSAL EVLLVEDVAL NREVAQGLLE RDGHRVMLAE
DAGPALALCR QRRFDLILLD MHLPGMAGLE LCAGIRRQLD GLNRATPIFA FTASIQPDMV
RRYFAAGMQG VLGKPLRMDE LRRALGEVGT SVPALAVDAA LDRQMLETHR RLLGRHKLAG
LLGNLLGSLD EQLPLLAEAL DQADLAEAAN IAHRLSGSCH SMGLVALGAG LGELEREALG
AAGVDPRAWG ARLGSLRRDG AEALRRAGFL GEADSAAG
