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Database: UniProt
Entry: K9NI10_9PSED
LinkDB: K9NI10_9PSED
Original site: K9NI10_9PSED 
ID   K9NI10_9PSED            Unreviewed;      1163 AA.
AC   K9NI10;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PputUW4_02521 {ECO:0000313|EMBL:AFY19716.1};
OS   Pseudomonas sp. UW4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1207075 {ECO:0000313|EMBL:AFY19716.1, ECO:0000313|Proteomes:UP000010397};
RN   [1] {ECO:0000313|EMBL:AFY19716.1, ECO:0000313|Proteomes:UP000010397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UW4 {ECO:0000313|EMBL:AFY19716.1,
RC   ECO:0000313|Proteomes:UP000010397};
RX   PubMed=23516524;
RA   Duan J., Jiang W., Cheng Z., Heikkila J.J., Glick B.R.;
RT   "The Complete Genome Sequence of the Plant Growth-Promoting Bacterium
RT   Pseudomonas sp. UW4.";
RL   PLoS ONE 8:E58640-E58640(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; CP003880; AFY19716.1; -; Genomic_DNA.
DR   RefSeq; WP_015095029.1; NC_019670.1.
DR   AlphaFoldDB; K9NI10; -.
DR   STRING; 1207075.PputUW4_02521; -.
DR   KEGG; ppuu:PputUW4_02521; -.
DR   PATRIC; fig|1207075.3.peg.2569; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG3706; Bacteria.
DR   eggNOG; COG4251; Bacteria.
DR   eggNOG; COG5278; Bacteria.
DR   HOGENOM; CLU_000445_127_1_6; -.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000010397; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd19410; HK9-like_sensor; 1.
DR   CDD; cd00156; REC; 2.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 3.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFY19716.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFY19716.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          500..720
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          772..885
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          894..1010
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1040..1157
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          389..490
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         821
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         943
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1090
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1163 AA;  130217 MW;  864D679B22B2E4BD CRC64;
     MTSASSVDEQ RFRKLLSRNI SLPLGLGLIS AVFFVSLITY LLSTIQWVEH TDRVINNANE
     AVKLTVDLET GMRGFLLSGD EHFLDPYETA KPRIAVALNT LLELTADNPV QTDRLLRLQA
     LQQEWASYAQ SLIDLQRSSG DYRSVVKAGR GKRLTDEIRK QFEEVIDSEQ QLRTTRNDEV
     RRTTVWSISL YLLFIAGVSG LLAYVGRRDL LSLSQSYSVN LASQQASAQR LEQQAWLRNG
     QTELAEQVLG QLSLNLLGRN ILQFCAQYLG TAVAALYVRE DHGGLRRIAS YGFSREQEER
     EQQIYSDEGI VGQVAQQARL IRLDEVPGDY FKVTSGLGDG LPRSVLVVPT SDDDRVNGVI
     ELGFLRPLND RDVALLELIA SNIGTSIESA RYRQRLQEVL AETQQLNEKL QVQQEELKTA
     NEELEEQSRV LKESQAHLET QQVELEQTNE QLAEQAQVLA EQRDAMDLKN SELNQAQIQL
     EERALELQRS SKYKSEFLAN MSHELRTPLN SSLILAKLLA ENPEENLTAE QVKFAESIYS
     AGNDLLNLIN DILDISKVEA GKLEIRPENT SVARLVDGLR DLFQPLATAK QLDFHVDLLD
     DAPQMLFTDR QRLEQVLKNL LSNAVKFTES GSVSLSVAAA PNDGIAFSIR DSGIGIEADQ
     HDSIFEAFRQ ADGTTNRRYG GTGLGLSISR DLAALLGGSI SVTSKPGQGS VFTLVMPQQY
     VEPGEEPVEP MRAVAVAAAP NAVPPTLSPL VAEVDIARFD DDRHKGPFTS RCILVVEDES
     NFAHILYDLA HELGYQCLVA HGADEGYDLA KAFIPDAILL DMRLPDHSGL TVLQRLKEHA
     ETRHIPVHVI SVEDRVEAAM HMGAIGYAVK PTTREELKDV FARLEAKLTQ KVKRVLLVED
     DDLQRDSIAR LIGDDDIEIT AVGLAQEALD LLRASVFDCM IIDLKLPDML GNDLLKRMST
     EDICSFPPVI VYTGRNLTRD EEAELRKYSR SIIIKGARSP ERLLDEVTLF LHKVESRLSH
     DRQKMLKVAR SRDRVFEGRK VLLVDDDVRN IFALTSALEQ KGAVVVIGRN GREAIERLNE
     VEDIDLVLMD VMMPEMDGFE ATVEIRKVPR WRKLPIIAVT AKAMKDDQER CLQAGANDYL
     AKPIDLDRLF SLIRVWLPKM ERI
//
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