ID A0A370DIB2_9GAMM Unreviewed; 1356 AA.
AC A0A370DIB2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DIZ80_03705 {ECO:0000313|EMBL:RDH84583.1};
OS endosymbiont of Galathealinum brachiosum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2200906 {ECO:0000313|EMBL:RDH84583.1, ECO:0000313|Proteomes:UP000254266};
RN [1] {ECO:0000313|EMBL:RDH84583.1, ECO:0000313|Proteomes:UP000254266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1464 {ECO:0000313|EMBL:RDH84583.1};
RX PubMed=30022157;
RA Li Y., Liles M.R., Halanych K.M.;
RT "Endosymbiont genomes yield clues of tubeworm success.";
RL ISME J. 0:0-0(2018).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:RDH84583.1}.
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DR EMBL; QFXC01000007; RDH84583.1; -; Genomic_DNA.
DR Proteomes; UP000254266; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
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; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; 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; 3.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000254266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..130
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 139..255
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 292..331
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 339..398
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 392..464
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 467..519
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 594..646
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 647..719
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 723..776
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 979..1205
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1233..1350
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1203..1230
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 188
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1283
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1356 AA; 154404 MW; 830ED1B40356D136 CRC64;
MNIETVKEQQ DVQYIYLTGS DELIIENIIK LLQQDNFIVN VFSNLSEMKQ ACEYKMPACL
VIEKDFKEDK EILNEISGIN NRFKSCLPIV LISQNNTMKT RLASARAGVS RFFCKPLDCE
KFLLTIIELT DQLNVNPYRV LCIDDNELML EFYESVLKEA NIECEMLSKP LQALDVLEKF
NPDIIVMDIQ MPECLGSELA QVIRQDDTWA QMPIIFLSSE VDLGNQLAAM NLGGDFFLSK
PVSVDHFLAA VNARVKRARQ IYQLNKNLQH VLRENKFQLA TMDEHDIVSC TDVTGKITNV
NDLFCEISGY SREELLGQNH RLLKSGLHPD SFYKEMWKTV SEGEIWRGTI CNHKKNGEEY
WVDSTIVPFL DNKGKPYKYV SARTNVTELR KSEERLNRSQ QFSKIGTWDW DITTGELFWS
DLIWPLFGYE KELIETTYEN FLAAVHPDDR QNVIDAVNNC VEKGSEYNIE HRVIWADGSE
RWVQESGDVV RSVDGKPLHM LGVVQDINTR KKAELDLQER EKQLREAQSI ARIGNWKANV
ISGELVWSDE IYRIFGYEPG SIKPSVEAFK KAVHPDDLAK LEESEKQAQQ TGLHDVIHRI
ILSDDSVRYV HELAQAETDE AGNLINLTGT VQDITDRIES EEKLHETEER FAFAVEGAGD
GVWDWDMQSN SMQFSETYMK MIGYTKNELA HKLDTWVKMV HPDDMARIQK SLQDYLQGRS
ENYSVELRLQ CKQGNYIWVL CRGTVVSRDQ GNRPLRMIGI HSDITERVEL LDKLSLQKSL
VDRLHHSATS FVEKSDFRKT MNGMLNTLLL LTESDYGFIA EVLTDDKGQY LKTHAITNIA
WNDETQLLYE NSIEDGIEFR NLNNLFGHIL ISREVVISND PANDSRSTGL PEGHPVMSSF
MGVPVFYGNE LIGVYAIANR ENGYDKEIQS FLRPFDITYG AIIHSKRMME LESENRKVII
DAKEEAENAN RAKSQFLSSM SHELRTPLNA IMGFSQLLKM EQLNESQNEN VNEITKAGGH
LLELINEVLD LSKIEAGRIE LSMDSIIIEE AISESFQLIT PLAQKRGIEI SIEHNGTEIS
FDQMINLQHA VRADHSRLRQ VLLNLLSNAV KYNNENGKII INYENSESNL IRVSITDTGY
GLSTDQQGQL FKAFNRLGAE QTEVEGSGIG LVITKNIIEL MGGNIGMSSA EGSGSTFWVE
LKSDELKINV DDLQDDSKLL KNEVENIMKH KYTVLYIEDN PANLRLVNQL LSRRSNIHMW
SAPEPLLGLE LAAEHKPDLI LLDINLPGMD GYEVLKQLKL REITRNIPVI AISANAMPRD
IEKGAKAGFD DYITKPINVT TLLETVDKKL SETIND
//
