ID A0A0P1FAW5_THAGE Unreviewed; 1004 AA.
AC A0A0P1FAW5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=kinE {ECO:0000313|EMBL:CUH65344.1};
GN ORFNames=TG4357_01811 {ECO:0000313|EMBL:CUH65344.1};
OS Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH65344.1, ECO:0000313|Proteomes:UP000051587};
RN [1] {ECO:0000313|EMBL:CUH65344.1, ECO:0000313|Proteomes:UP000051587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH65344.1,
RC ECO:0000313|Proteomes:UP000051587};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYSA01000016; CUH65344.1; -; Genomic_DNA.
DR RefSeq; WP_058262548.1; NZ_FOFW01000010.1.
DR AlphaFoldDB; A0A0P1FAW5; -.
DR STRING; 53501.SAMN04488043_11099; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000051587; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 3.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 4.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CUH65344.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051587};
KW Transferase {ECO:0000313|EMBL:CUH65344.1}.
FT DOMAIN 14..53
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 649..862
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 882..998
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 931
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1004 AA; 110730 MW; D389541C58BF0665 CRC64;
MNMTPDMQTP CPIIREAMDA LAEGVVLFDK ARNLVFANHS YAEMLGYHSN QLMPGTPMQD
IISSAVENGH IRILHGAQKG ISTFLATLDT LDSAKIEIQV SDGTQREITL TRLSDGGIVG
SVKDVTKQQT TEAQARDLLN KAIDAVDVGI ALIDDDETLV FANRKFTEIA DPAGQILRQG
MPIRDTFEKA VASDLFLLPD GISPTDMLEA LDTLLRTAAK GFSLTKVNGR EIVGKFYETV
LQGRLLTLED VTDQLRAEQL FTDTVARLPV GVAIEQASGQ LSHCNDAFSE PFGYRADDLL
KLTDAQRFKT LAPMIASISG EDVGRRGAEF FAAAIRSQRE TLAPMEICFR NGRHYLVERA
VTEGDGRVVV VTDTTALKEA EERSLRTLND TIQSLEEGLA VFDKDSRFLL GNRQWRKLFF
DDIALPREGE LLSDLWARLI GAGVFSLPEN ITANAYLETL NHFSRAHQMK ETLLLRNGRT
IVASVHGTEQ EGYLLSFMDV TEQRRAESEQ READLLLRKI VDACPANFLV SRVDDGKIIY
CPPPSRERFG KIESALSFFL TPDDRQNYLD ALLPTGSLDD YRVQFQRADG SIMQGLTAAR
VTEYKGEQVI VSSTRDISDL LAMQEELQQQ RDAAHQTEKL SALGELLAGV AHELNNPLSI
IVGYAQMLSG RLEDEVLAKR VDRIGEAADR SARIVRAFLA MARQRPTTVE PCSLNDIALT
ALDVAGYGLR AMGTNIEMQL DDELPEISGD PDLLVQVFSN LIINAEHALA PLGQSGLLLI
RSFFDTENNQ SVVEIRDNGP GIPEAIHARV FEPFFTTKDV GKGTGIGLAF SHRIIVAHGG
QLDLESKEGK QTSFFVRLGV HEERDVIVTR EQTEAPAATS SRVLVVDDDE SVGELICDIL
EELHCEPVLV ADAATALDLL GHETFDVVLS DFKLPGMNGA DFYKAIQQTL PHYANRVGIV
TGDTLDEDVF RFLSEVQRPY IEKPILRQDL SDLLKRLSES GNGT
//
