ID A0A0U4VIU9_9PSED Unreviewed; 1178 AA.
AC A0A0U4VIU9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=APT59_01810 {ECO:0000313|EMBL:ALZ82999.1};
OS Pseudomonas oryzihabitans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=47885 {ECO:0000313|EMBL:ALZ82999.1, ECO:0000313|Proteomes:UP000064137};
RN [1] {ECO:0000313|EMBL:ALZ82999.1, ECO:0000313|Proteomes:UP000064137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-56511 {ECO:0000313|EMBL:ALZ82999.1,
RC ECO:0000313|Proteomes:UP000064137};
RA Harhay G.P., Harhay D.M., Smith T.P.L., Bono J.L., Heaton M.P.,
RA Clawson M.L., Chitko-Mckown C.G., Capik S.F., DeDonder K.D., Apley M.D.,
RA Lubbers B.V., White B.J., Larson R.L.;
RT "Annotation of Pseudomonas oryzihabitans USDA-ARS-USMARC-56511.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP013987; ALZ82999.1; -; Genomic_DNA.
DR RefSeq; WP_059313289.1; NZ_CP013987.1.
DR AlphaFoldDB; A0A0U4VIU9; -.
DR KEGG; por:APT59_01810; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000064137; 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; 1.
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:SF79; HISTIDINE KINASE; 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:ALZ82999.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000064137};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 500..719
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 787..900
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 909..1025
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1055..1172
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 389..496
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 836
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 958
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1105
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1178 AA; 131510 MW; 8068F63DD41FEE09 CRC64;
MNRESPLDQK HFSKILKRNL SLPLSIGVFS AIFFIAIIYY LLRVTQWVEH TDRVISEANA
NFRLVVDLET GMRGYLLSGN TSFLQPYERA LPEVEPQLDE LKNLVSDSAV QIRRLERIAA
VHREWRQYAS QVIEARRLGG DFQTPLSDGQ GKNRIDSIRR DYTDFIAYEE QMRAERTETA
SRMTVVFVAA FLIVSLLLSG IMAFFGRREL MRLSATYTGL LDQQAEHTEN LERQSWFRSG
QNQLSEAVIG QAALAPLGQS ILQFLARYLG AAAGALYVRL DDGTLERVAD YALDDEGRRR
RQRLAPGEGL AGQAVLEGRA VALDQLPADY LKVNSALGER QASAALIVPI ENDGRVNGVL
ELGFLRALQP QDKELLTLIA DSIGSSVEAA RYRQRLQQVL AETQQLNEEL QVQQEELRTA
NEELEEQSQA LKESQVHLEQ QQAELEQTNE QLSEQAQELL QQRDVLDDRN NRLNEAQQLL
EDRARELERA SQYKSEFLAN MSHELRTPLN SSLILSKLLA DNPAGNLSGE QVRYAESIYS
AGNDLLTLIN DILDISKVEA GMLEIRPEQM SVRRLVEALK TAFEPVAQNK GVGFEVELDA
QMPTSFFSDR QRVEQILKNL LSNAFKFTEH GQVTLRLSLE DGQPSFAVRD TGIGIAAEQQ
ELIFEAFRQA DGAITRRYGG TGLGLSISRD LALLLGGTLS VTSQPGEGST FTLRLPLEYQ
EAAAPTLPVT PVSAPAVATT PVSAPMPLAT LAATPRPSAP APITEAAAPV GAAFADDRDN
WPYPDRRVLV IEDEVPFAQI LFDLAHELKY SCLVAHRAEE GFAIALEYRP DAILLDMGLP
DHSGLTVLER LKENPLTRHI PVHVVSASDR VETAMHMGAV GYAIKPTTRD ELREAFTRLE
SKFAAGIKRV LLVEDDALQR DSIAKLIGDV DVEITAVEMG SQALDLLRDE VYDCMVIDLK
LPDMEGGELL ERMASEDICS FPPVIVYTGR SLSRDEEATL LKYSRSIIIK GARSPERLLD
EVTLFLHKIE ADMPLDRQRM LESARSREKA FDGRTLLLVD DDVRNIFALT SALEQKGAKV
EIARNGLEAL EKLDNSDTID LVLMDIMMPM MDGYEAMREI RKRPHMKKLP IIAITAKAMK
DDQERCLAAG ASDYLAKPID LDRLFSLIRV WMPSLERL
//
