ID A9BLH7_DELAS Unreviewed; 1177 AA.
AC A9BLH7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Daci_3831 {ECO:0000313|EMBL:ABX36462.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX36462.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX36462.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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; CP000884; ABX36462.1; -; Genomic_DNA.
DR RefSeq; WP_012205656.1; NC_010002.1.
DR AlphaFoldDB; A9BLH7; -.
DR STRING; 398578.Daci_3831; -.
DR GeneID; 24118482; -.
DR KEGG; dac:Daci_3831; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR eggNOG; COG5278; Bacteria.
DR HOGENOM; CLU_000445_127_0_4; -.
DR Proteomes; UP000000784; 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; 2.
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:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 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:ABX36462.1};
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:UP000000784};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABX36462.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 482..702
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 786..899
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 908..1024
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1054..1175
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 382..458
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 835
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 957
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1108
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1177 AA; 129293 MW; 82A5CEB95D464FA1 CRC64;
MPRSSSHQTT QRFAVPWTLV AGFGAAALAT LVIAFVNFRS SEARGQAVNA MDRTTLAMRQ
LSQLNASLKD AETGQRGFLL TGDQAYLQPY QQARDVLQKQ LEALKARTSS DSVQHRLLDQ
IEDISTQKLR ELQETIDLRK AGDLDAAMAL VRLDVGKNAM DRLRELIDDL YTRQTRELEQ
RRQLWVEAST TSTYYSWGGS LILLGLILAS AALTVREYRV KARQSWVTSG LSGLGQQLQG
DRRLEDLGQK ALEYLATYLR AEVGAGYVVD CADGGLRLFG GYALPRERLQ HKLLPGEGLA
GQAVASRKLL HVRDVPAQHL PISSGTGQSS PLQLMVAPAM ENGEVFAVIE LGFLRGVSEA
ERSLLERASE MLAVAIRSGL DRSRLETLLE ETRRQSEELQ AQQEELRVSN EELEQQSRIL
QESQTQMEHQ QSELEQTNAH LEEQTQQLEY QREQLLRAQG ALTDKAHELE LASQYKSEFL
ANMSHELRTP LNSTLILAKL LADNKPGNLQ ADQVKYAQTI HAAGSDLLAL INDILDLSKI
EAGQVSVLVE PMTIATALQA LMEPLRPIAR EKGLELTWTV DPGVPASMQT DPMRLAQVLK
NLLSNALKFT AKGSVGLQVS RVPGGMLAFA VRDTGIGIAE QQQQFIFDAF RQADGSTHRK
FGGTGLGLSI SRDLAGLLGG TLTVSSTPGQ GSVFTLTVPV ILELVEPGQA LAAAPLPRPA
RESLANEQTQ TQVSSPASVP AVASAHVAPA APAFAPAMSP AMSAPMLSPT SSAADALRKS
GQSGRRILVI EDDRRFADIL SELAREMDFE CDVASTASDG LAMAASNQPN AIVLDINLPD
FSGLGVLDQL KRNPVTRHIP VHVVSVADYS QEAMGRGAVG YALKPVKREE LVHALKRLEA
KFTQDLRRVL VVEDDERQRE SVRHLLSRSD VDIVCAGTAA AALEHLRGAT FDCMVMDLNL
PDISGYELLQ RMTDQDDVSF PPVIVYTGRA LSRDEEQQLR RFSKSIIIKD ARSPERLLDE
VTLFLHQVES ELSAEHRQML QVARSRESAL EGRTVLVVED DVRNVFALSS ILEPTGIRVE
IARNGREALE TLEARGTAQA GIDLVLMDIM MPEMDGYTAM REIRNRPQWR RLPIIALTAK
AMKDDQEKCL AAGANDYIAK PLDVEKLLSL VRVWMPK
//
