ID A0A3F2UZ67_9GAMM Unreviewed; 891 AA.
AC A0A3F2UZ67;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D6160_18545 {ECO:0000313|EMBL:RLP52893.1};
OS Ketobacter sp.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ketobacteraceae; Ketobacter.
OX NCBI_TaxID=2083498 {ECO:0000313|EMBL:RLP52893.1, ECO:0000313|Proteomes:UP000280615};
RN [1] {ECO:0000313|EMBL:RLP52893.1, ECO:0000313|Proteomes:UP000280615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BinD {ECO:0000313|EMBL:RLP52893.1};
RA Xu J.;
RT "Metagenomic reconstruction reveals the metabolic diversity of the novel
RT genus Ketobacter and the trajectory of genomic evolution within the
RT Alcanivoraceae family.";
RL Submitted (SEP-2018) 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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLP52893.1}.
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DR EMBL; RAHY01000023; RLP52893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F2UZ67; -.
DR Proteomes; UP000280615; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RLP52893.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000280615};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 156..314
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 537..754
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 774..890
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 751..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 823
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 891 AA; 102299 MW; A74E4F887269237A CRC64;
MTLDVDKLAF EHCEDEPIHI PESIQSYGYL FAINQENHRI EIISENVIDL FNLQGDIVGT
DFFALLDEDQ EGVDFILETY QRARNRKTRL PIKIKFKETL IRQLSDRDFF AVIYNSADRL
IIELEPAAKF RKAYTAEHYI KIYAMSIAPK FKAFDSLNEM AQEIVETIKY ITDMERVVLY
KFNDDDSGKV IAEAKNNEVD AYLNLYYPAS DIPPQARELY KKNWVRLTPN VDLAPSRLIP
TTQDSGREPL DLTQSLLRTL SPIHCQYIRN QGLRASFSMS LVTHDRLWGL ISCHSRNPTY
IPQDVRLQCE NLSQLFSWHL YAKEEELFFK QKELADRSIE AMLDKISPSF PIVSVFSQHE
EEVLRLMDAD GFIFYSDQEV ISLGQTPDLN IVQDMYNRVD THDRKPFITN SIDKKWGTSE
QLNGIYGVML IPLLEKRSYF TAWFRKERVY IQKWAGSPDE KNVDASKRER LMPRTSFQVH
IKEVAGASKE FDQNDVDMAS RFNRMFLAHA LEVQEKMRKN MNDLEQQDRH KNEFLATLAH
ELRNPLSPIS TGVSLLEISD KSDVREKVLA TIKRQVGYMT KLIDDLMDVS RITQGKIKLD
IQHIVVQEVL SNAVEIIESL MREKGHQLVL DMPEPPVYIH GDSARLSQVF SNIINNAIKY
TDRNGKIEVS LQLNERHISV KIKDNGLGIP KEKLKDIFSM FTQVEAHSTH TKGGLGIGLT
LVDRLVKLHH GEVIARSDGE RQGSEFEVIL PRANESSQQQ TSTASTEDAD RKQRVLVVDD
NPDVTELLNI LLQNAGHKTA TASNGREAID LFKQFKPDFA LLDIGMPDID GYELCKILRK
LPEAKNTIFL SQSGWGNKEY VDRALEVGFT RHFVKPLDFS VLQAALNKYA K
//
