ID A0A498DMS6_9PROT Unreviewed; 2274 AA.
AC A0A498DMS6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D8Y20_01830 {ECO:0000313|EMBL:RLL55665.1};
OS Mariprofundus sp. EBB-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=2650971 {ECO:0000313|EMBL:RLL55665.1, ECO:0000313|Proteomes:UP000270267};
RN [1] {ECO:0000313|Proteomes:UP000270267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EBB-1 {ECO:0000313|Proteomes:UP000270267};
RA Lopez A., Barco R., Canela R., Emerson D., Tully B., Abuyen K.,
RA Broomell S., Albino D., Beraki S., Dingmon T., Estrada S., Fernandez M.,
RA Amend J.;
RT "Genome Sequence of Zetaproteobacterium sp. EBB-1: a novel, marine, iron-
RT oxidizing chemolithoautotroph isolated from an iron-sulfide mineral.";
RL Submitted (OCT-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 -!- 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:RLL55665.1}.
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DR EMBL; RCFQ01000002; RLL55665.1; -; Genomic_DNA.
DR Proteomes; UP000270267; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 8.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 2.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 10.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 10.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00571; CBS; 4.
DR Pfam; PF13185; GAF_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 4.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 4.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 4.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 10.
DR SMART; SM00091; PAS; 10.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
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); 10.
DR PROSITE; PS51371; CBS; 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 7.
DR PROSITE; PS50112; PAS; 7.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
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:UP000270267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..65
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 73..131
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 138..193
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 202..263
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 280..354
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 409..479
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 483..533
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 747..792
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 795..847
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 924..976
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 977..1047
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1050..1102
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1103..1173
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1164..1226
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1547..1592
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1595..1647
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1768..1818
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1843..1897
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1910..2137
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2157..2273
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 2208
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2274 AA; 255012 MW; A015E3BEF4AA8ADF CRC64;
MNLTIADILT RQVLTVVPET TLAAAALLMT EKRISCLVAV TDGKPVGVLT EADLVRVGHL
RIDAEHTAIS DFLSQPVISI ATNQSIYAAF DFLLEHHVRH LVVVRPDGRL EGLLTFTDIL
KAAEFDDFLP VKSISSVMSR NVKTMQAEDS LHEAMATLSD LHISCVVIAE QGKAIGIFTE
RDAARLVAAD RDLDNLCLAD VMTTPLITMA ADDSLLDASI LMREKGFRRL VIVDEAAHPK
GVITQFDVIR GLEGDTIRHF KQLHAKTEER LNESSRLLAE KSELERIVDA SSAVLYRCEW
IGEQFVGTYV SPSVTSLLGY DRQECLQPGW WSDHLHPDDR YKIEQNMPRL FETGEVEHVY
RFAGKTGEYR WIRDHLRLRK GVDNRPDELI GSWLDITDSR KIEQRVFESE EMYRSLVEQS
FDGIVILDAE GSMLFANDAS AKAWGGTVEE LSDQAFLDVI HPDEKARMQL YFKQRMDGAV
QQEVYETRMV RKNGDTLWVE LSGRLITWQK QPANLLTLRD ISERKLAEME EENRLLLNSA
SADAMSAFIA DKPLQQVFDP LLKLLLDATQ SAYGFIGEML HSDAGAPYLK TFAVTDIAWN
DETRSFYDEN VAKGLEFHNL DTLFGAVLSG EEIVVSNDPA NDARAGGIPK GHPPLQAFLG
LPVKVGSKML GMIGLANHPE GYDQAMIDRL APLLDVIANI IVSMRSKRAH QQAEKALQDS
ESRLLASQAI SQTGTWDWNP QSGDLIWSDE TYRIHGYEPG QVKPSYELFL EHLHPDDRPM
LAAAVEAALN DEQFYSLDCR LQSVDGKEKI CHAQGGVEFD QDGQPLRMLG VFQDVTERKQ
VELSLDKSLQ RMDFLLKSTP VVIYSCQPEP PFAASFVSLN VVDQLGYDAA QFTQQPDFWA
NHIHPDDREQ VIAEMPRLFE NGVHAHEYRF QHKDGSWRWM SDELRLTYND AGEPTEIVGY
WIDITARKQA EKAISISEKK FRSLFEESRD MMHMAGPDGR IIDVNQAELD TLGYSYEEMI
GKPLEELVCP EYHEITMPKF SALMQGQSVP VYESAMHAKD GTCVHVEVSA VPQLDEHGDV
TASRAIIRDI SARKLAEKQI QDLYQQYESV TGSIADVLYY IDCNLKLVWW NRHLETITGL
APQDLQGRNA DTFFAEADLP KLKQAIERTF SEGEAEDELF FNTIHGAVLH HFKGSLLKDG
QGNVLGITGV GRDMTAIKQG EAQLKRREQQ LSVLAEAGRV INEQLGEIEI GRSLATLARR
LVECESGAVG FYRNEKICFR EYLRAEESIP IALDFPAGYG VPGFVLETRA PYISADAMND
EHVIPEIQQS LVFMKLIDVP ILDATGNILG CVEMHDRLDG HDFDDQDLEM LQGLAGIVAA
ALVNARQQNE IEQAAQRMRL ILDAEFDAIV VQQDEKIVFS NKQAQQLFGY ASFEETLGEN
AMLAFLPAQR NLAARIARRV IRNNKPTERV EMMGVSRSRS EPFPMEIASA PIQWSGKPAV
VSIVRDITER KRAQTLLNQA YSRHEMAQRI AQLGHWDFDH INDRLEWSEG VYRIFGLDKA
DVELSYEMLQ QLVHPDDREQ LVRVFELSLE NRASFELEHR IVLPNGEQRW VFEQCETEFS
KDGTPIRSLG TVQDISERKH HLEQIERERA AMRAILNNLP FMAWLKDEEG RFIVVNDLFA
EACGAESAEA LVGKSDLDLW PEALATGYMQ DDREVMDSAT PKQVQELVEG KDGKGPISFE
TFKSPVFGSD GRVVGTAGMA LDISDRLERE KQMRLLESAV GSVNESIIIT NVEGVIVYVN
PAFTSNTGFD RDYAIGNSPA ILNSKQQSKG FYELFWQTIM AGEPWSGRIL DRKKDGTIFP
VHLSVAPIFD EPGEITHFVA VHEDLSSAEA MQKKMMQTQK MEAVGTMVGG LAHDFNNMLA
SIVGNFYLIR MQHKDDEKLI KRIEGMEKAT HHGANMIQQM LTFARKDRPD MHVLSLNSYI
KEAHKLAAGS VPENVHFKLD IGRGCDCNVK ADATQLQQVL LNLVANARHA IRDLEHGEIR
VGLDRRQPPE HVLSGNVELT ADSSWCRIFS EDNGCGIREK DIERVFEPFF TTKAVGEGTG
LGLAMVYGAV QNHRGLIDID STLGEGTTIS IWLPEYAQKA AEVTGVDEAA VDGAGQVVLL
VDDERELRHV LAEVLQHNGF KVLQAVDGEQ AVETYERYSD DIDLVLMDVV MPNKGGVMAA
KEIRAMNANV PIIFQTGYGE QTQLDAAASI NNSDSLHKPV QIPKLLKKIT EWIK
//
