ID B8FAJ2_DESAL Unreviewed; 872 AA.
AC B8FAJ2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Dalk_1590 {ECO:0000313|EMBL:ACL03288.1};
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfatibacillaceae; Desulfatibacillum.
OX NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL03288.1, ECO:0000313|Proteomes:UP000000739};
RN [1] {ECO:0000313|EMBL:ACL03288.1, ECO:0000313|Proteomes:UP000000739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL03288.1,
RC ECO:0000313|Proteomes:UP000000739};
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL03288.1; -; Genomic_DNA.
DR RefSeq; WP_012610722.1; NC_011768.1.
DR AlphaFoldDB; B8FAJ2; -.
DR KEGG; dal:Dalk_1590; -.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG3322; Bacteria.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_009587_1_0_7; -.
DR Proteomes; UP000000739; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 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 Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR007892; CHASE4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF05228; CHASE4; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 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; 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; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACL03288.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000739};
KW Transferase {ECO:0000313|EMBL:ACL03288.1}.
FT DOMAIN 368..439
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 442..493
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 513..737
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 COILED 341..382
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 805
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 872 AA; 96713 MW; 5AA836FC69D1D9DC CRC64;
MKLRSKLLTI LLASALLFGV TQGLIQHYII SPRFAALERR EAKKDLLRCV RTLETETEHL
KALTHDWASW DDTCDFIKGG GPDYEESNLA LETFVDASLN AICFFDGNGD LFWGKAVDIE
TGAPLQIRLL SAGKLLRGHP LFLDASSFVY QKDISKSGII RTEYGSMLVA SLPILNTENK
GPVMGTMVMA RLITEAMKDK LRDQTQVPFD IKMIDPGYAG ADSGGEGNLL LKPLDENTLQ
ASMILKDITG KPCLELSADL PRDILQQGLA SMRTARGVKV AAGILFLALL IWLLEAAIVR
PVVRLTGRML VARKTRELPG KVFEGRKDEI GTLENEFDRL LETVLSQSKE LEEELAAKQN
LAEKFKENFQ KYKLLAENLK DVVATITPDG YIQYCSPAIT EFSGHTVEEV EGRHVFGFMP
ENSDRERLIE LVDQIAKYGD SRSLEYLMKA KDGTAFHVES TAKPIMENGK LVLLHCVFRD
ISERKKVEDE KNRLEAKLQM AQRMEALGAL IGGIAHNFNN VLAPIMGNTE LAMLDVPEDS
QAYKNLQQVL VASEKAKKMV RQILSFSDHG GEDPAMIDIE DVLEETYGLV RASLPSSIEI
RKEVEKISGL VYADPKELQR VLMNICANAA YAMKELGGVV DISLEEQDIT EFDLDHSRKI
KPGKYVKLSI SDNGPGMESE VIQRVFEPYY TTKPVGEGSG MGLSEAFALI SKYGGEIKAY
SEPGMGASFY IYLPLMAASS KTHSKETLPQ GSERILLVDD EEAVLAMTRQ MVEHLGYKVT
AVDNSPQALE IFEADPQAFD LIMTDMTMPY VTGDSLANRI LSIRPEMPII LCTGFSERLS
REQARNIGIK AYVTKPVVMA QIAGIIRSVL DQ
//
