ID A0A090AGM6_9GAMM Unreviewed; 1054 AA.
AC A0A090AGM6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-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=THII_0070 {ECO:0000313|EMBL:BAP54367.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP54367.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP54367.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
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 -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; AP014633; BAP54367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090AGM6; -.
DR STRING; 40754.THII_0070; -.
DR KEGG; tig:THII_0070; -.
DR HOGENOM; CLU_290331_0_0_6; -.
DR Proteomes; UP000031623; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 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; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAP54367.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031623};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 292..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 313..365
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 380..597
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 644..761
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 801..927
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT MOD_RES 694
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1054 AA; 119375 MW; 0E71AAAEF55D7A5B CRC64;
MGSFLLLIIP ILIAMSVSDY LNAKADLENA YKMLQQQTEN NILNAIKLVD AGHKVLERFI
DKEMRDAFVT FIDAYEVSAR NPKKMEFEDL KKQLGGKMDL YVINADGVVE YTTYTKDLGL
DFKKWPDVFA FITKIRQQNH FASGGFATEA RTGSIRKFAY MPTPDHNYLL ELGLFSDEFS
DLMGGLDVVQ ITARLKTLNP SLNQVRIFSR HGHSLGDPNY KVNEETAKII KTVYDTKKTT
EIEDKIRKRY TRYIFVNLKD EDVDISTDPS KVIELTYNTK LIDEGLQRTA SFHFILSIVA
IVLSILFTFI ISAWITRPIQ SIVNSVNIIA EGQLDHSIEV ETNNELKLLK QSITKMVTSM
LRYINDLRVL DKLKDDFLSN TSHELRTPIN GIIGIADSLI DGAAGPLPDK AVENLSMIVL
SGRRLSNLVN DILDFSKLKH KNLELQIKPL EIKVVVEVVI TLSKPLIGRK KVELVNNIED
DILVDADENR VQQILHNLIS NAIKFTDAGI IEIASTNYHD YLMISVKDMG VGIPPDKLEM
VFNPFEQADG SIAREYGGTG LGLSITKQLV ELHGGEISIK STLKKGTTVS FTLPLSTSTI
VDRNTDMSTM LSRIRHLPPI EVSVERDKEE INPDHTQQGR EQFHILIVDD DPINLQVLEN
QLRLENYAVT RAHNGQEALT AIDSGTQFVI ILLDIMMPKM SGFEVCRIIR ERYSITQLPI
IMLTAKNQVS DLVEGMQAGA NDYLTKPFSK GELITRIKTH IQLSKVNMAY SNFVPLEFLK
LLEKDSIVEV RLGDHVQKHM AVLFADIRSF TTLSESMTPK ENFDFINAYL GRVSPVIRKH
HGFIDKYIGD AIMALFPESA DDAVQASIEI HQHLDIFNQE RQQKNLQPIH IGIGLHIGTL
MLGTIGEEKR MEGTVISDAV NLASRLEGLT KLYGASIIIS QQILTELTDK EQHHYRFLGK
VRVKGKQEPV KIFEILDPEP DEVREKKIIL QPTFNQAIEA YYQKQFQHAY QLFEHILQQL
PTDKAASFYL ERCEYYIKQG TPPDWEGIEA LAQK
//
