ID T0K1E6_9SPHN Unreviewed; 992 AA.
AC T0K1E6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=M529_20160 {ECO:0000313|EMBL:EQB30379.1};
OS Sphingobium ummariense RL-3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1346791 {ECO:0000313|EMBL:EQB30379.1, ECO:0000313|Proteomes:UP000015523};
RN [1] {ECO:0000313|EMBL:EQB30379.1, ECO:0000313|Proteomes:UP000015523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL-3 {ECO:0000313|EMBL:EQB30379.1,
RC ECO:0000313|Proteomes:UP000015523};
RX PubMed=24233594;
RA Kohli P., Dua A., Sangwan N., Oldach P., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium ummariense Strain RL-3, a
RT Hexachlorocyclohexane-Degrading Bacterium.";
RL Genome Announc. 1:e00956-13(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};
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:EQB30379.1}.
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DR EMBL; AUWY01000121; EQB30379.1; -; Genomic_DNA.
DR AlphaFoldDB; T0K1E6; -.
DR STRING; 1346791.M529_20160; -.
DR PATRIC; fig|1346791.3.peg.3895; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR Proteomes; UP000015523; 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 CDD; cd16919; HATPase_CckA-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd18161; REC_hyHK_blue-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000015523};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 365..438
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 440..492
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 505..731
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 754..870
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 877..989
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 330..365
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 805
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 928
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 992 AA; 108013 MW; 535A20F55A332156 CRC64;
MFVAAERLAR ARSFEQIVEV VRSAAREIIG ADGITLVRCE GDECHYIAED AIAPLWEGQK
FKLSECVSGW VMQNGKPAVI PDIYTDERVP QAAYRPTFVK SMAMMPVQAG ASRASIGAYW
ARANAPDQPA LDQLQRLADF VSAAMDNVAL QNGFQLLNRT GAAVAAERDL DRIVQLITDA
GVELTGAEFG AFFYNLVNEK GESYMLYSLS GVPREAFSKF PMPRNTAVFA PTFSGEGVVR
SDNIRLDPRY GHNTPRKGMP EGHLPVTSYL AVPVVSRTGE VHGGLFFGHH REAQFTPEHE
TAVLGIAGHA ATAIDNARLY QSLERELIAR RAAEAALTDL NATLEKRIEE RTQEIRAAYD
KLKESDRRFR ILVNGVTDYA IYMLDTEGQV TNWNAGAERI KGYAADEIIG RHFSTFYTER
DREAGKPAQT LDTATRTGKF EAEGWRVRKD GTEFWASVVV DAIQDEEGKL IGFAKITRDL
TEKRFVDEQL RQSQKMEAVG HLTGGIAHDF NNLLTIITGN MDIAARALDK NEGIARAQKA
IGNAMKGAER AGALTQRLLA FARRQPLSPK PLDLDKVVAG MSDLLNRSLG ELVKLEIVTS
PGLWPVEADP NQMENALLNL AVNSRDAMPN GGTLTIETAN AHLDTAYSAA HAEVPAGNYV
VVAVSDTGLG MPKEHLVRVF EPFFTTKEVG RGTGLGLSQV YGFVKQSGGH VNVYSEEGRG
TTVKMYLPRF TGELNAVTDV ELGRLDGPGA AGETILVVED DDEVRAFSAE VLRELGYTVL
EAADGTAALR ILEQPGVEVD LLFTDVVMPG MSGRELSDEA RKLRPALKVL FTSGYTRNAI
VHGGRLDPGV ELIPKPFTSR ALAERVRELL DAGKCRRLLV VEADQTLRLL AAEAFAAAGY
HAELAGTAGE ALGVLRAAQG RFDGIVIDGE LPDKDGFTLL SEIRRLFADL PAVITVSAGD
SRAINDPRAV RIEQPFSATM IINALTSFER QG
//
