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Database: UniProt
Entry: A0A285NV50_9PSED
LinkDB: A0A285NV50_9PSED
Original site: A0A285NV50_9PSED 
ID   A0A285NV50_9PSED        Unreviewed;       636 AA.
AC   A0A285NV50;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05660463_01939 {ECO:0000313|EMBL:SNZ11746.1};
OS   Pseudomonas sp. URIL14HWK12:I9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1261633 {ECO:0000313|EMBL:SNZ11746.1, ECO:0000313|Proteomes:UP000232228};
RN   [1] {ECO:0000313|EMBL:SNZ11746.1, ECO:0000313|Proteomes:UP000232228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URIL14HWK12:I9 {ECO:0000313|EMBL:SNZ11746.1,
RC   ECO:0000313|Proteomes:UP000232228};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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};
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DR   EMBL; OBEM01000003; SNZ11746.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285NV50; -.
DR   OrthoDB; 9797243at2; -.
DR   Proteomes; UP000232228; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SNZ11746.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000232228};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          188..240
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          269..491
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          519..635
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          235..262
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         568
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   636 AA;  70181 MW;  2C3544CD47F1B9E9 CRC64;
     MSFRWRGDIH ARTHIISLGP ALLLTLLLIC FFTFVRIQDL RQEMNHTGQL IATQLAPAAE
     YGVVTASPQV LEGLLRGTLN IPHVRFLEVQ DPTGKVLARV EQPGDSPPAP SMEMFQAPIR
     VQRFALADAD PGLEGPQPLH ADDYLGRVLV GMSDDGFNQR QQEILLKAGV LALFTLLITF
     LLARRLARSL SQPISDMSEA VKAIRRGEFR TTLPEERDSE LGELARHIND LALGLEQASR
     EQREAMAQLI QTREEAERAN NAKSEFLAMM SHELRTPMNG VLGMLQLLET TPLSEEQAEY
     ATLATQSTEH LLKVINDILD FSRIERANLE LEHISFNLGE LIHSSVGAFA HTAQQRGLAL
     ELVLDETSQS WNVNGDPTRI RQVLVNLIGN ALKFTEHGVV RVQASCQALD DQLTWLTCSV
     SDTGIGIGAP VLESMFIAFR QADSSISRRY GGTGLGLPIA RTLAERMGGT LRARSEEGRG
     SVFTFEIPLA LHRTEGNHHL AEPLPPPQPK VKVEPAVARV LLVEDNPVNQ TVIEAMLRSL
     GHSVTVVGDG ATALEQVAQQ HWDAVLMDCR LPVLDGYEST RRIRRLPDRQ QLPVIALTAN
     ALLGDREACL AAGMNDYLAK PFKRADLQQL LGRWLG
//
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