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Database: UniProt
Entry: A0A2Z2P178_9GAMM
LinkDB: A0A2Z2P178_9GAMM
Original site: A0A2Z2P178_9GAMM 
ID   A0A2Z2P178_9GAMM        Unreviewed;      1083 AA.
AC   A0A2Z2P178;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=IMCC3135_16060 {ECO:0000313|EMBL:ASJ73294.1};
OS   Granulosicoccus antarcticus IMCC3135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Granulosicoccaceae; Granulosicoccus.
OX   NCBI_TaxID=1192854 {ECO:0000313|EMBL:ASJ73294.1, ECO:0000313|Proteomes:UP000250079};
RN   [1] {ECO:0000313|EMBL:ASJ73294.1, ECO:0000313|Proteomes:UP000250079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3135 {ECO:0000313|EMBL:ASJ73294.1,
RC   ECO:0000313|Proteomes:UP000250079};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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; CP018632; ASJ73294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z2P178; -.
DR   KEGG; gai:IMCC3135_16060; -.
DR   OrthoDB; 9770473at2; -.
DR   Proteomes; UP000250079; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd02205; CBS_pair_SF; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 3.
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; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
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); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
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:UP000250079};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          332..402
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          448..502
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          522..572
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          573..643
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          646..699
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          719..944
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          966..1082
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          683..710
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1017
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1083 AA;  121454 MW;  0D605BF6405CF0D1 CRC64;
     MTQLTVSLKE LPLRKFLQVA PDTLLSEAAR QMDNDGLDTA LVMQGQNLLG ILGSRDRLRA
     FHQQTPPNTP VRELMNSAHC SLKQNTFITD ACSHLLQHAA SELVITNELG MPLGLIGESE
     LLQYITPFLT NDTQANKDWV LQHASKRMEA DKQLHTLKRQ TDLLSRFAAA LINLPADDID
     PVVNHALMEM GELVQVDRAY IFHYDFDTDT ACNTHEWCAS GISPQIHNLQ VLPIQELSDW
     VCKHKRSENV VVDDFNLLPP GMMREVMEQQ DIKSMVCLPI LGNEGCIGFL GFDSVRSKRQ
     YAPEDLEVLE LFARTLANYR ERLIAEQKLA NNEANFHAFF DQTQDLLFVL SQQGDIVQCN
     TQATQRLGFS MEELYGKPVL QLHPDENHTE AAQIVADMAK GKTDCHAIPM QTRFGQQVPM
     ETRVVAGQWN GIPALFMVCR DLSDITSSEE KFSKAFHLSP MPMAISDVQN GTFLEVNEAF
     FHVTGYDTHE VVGKNVAAMN LFGDLKLWGH IIEQLQQQGQ VNNIEFPLRT KQGDIVYGLL
     SAALLELQGR QVMISQLLDI TARKTAEEAL VNERLLLRTL INSQLNLVWL KDPEGAYLAC
     NSRFESLYGH TESEILGRTD IEFVNQEWAE FFRKNDHLAI KAGKPRINEE TLTFASNGYQ
     GLFETTKTPI FNGQQKLLGV LGVAREITHA RHAEQERRRM ERELHQSRKM EALGQLTGGV
     AHEFNNMLAI ILGYKDLLQA KLDPSTDSSI NIWLDHIDVA GVRAKELVRQ LLSFSRPNEK
     QPKRINLEIG VRKAIALSQS SLPSSIEIDY RPDPELPDVQ LDIGELQQML TNVLVNARDA
     MDGKGRIEVT LQHTRHTEQE CQLCHTLIEG YWVELCIADD GPGIFPEQLS RIFEPFYTTK
     AVGKGTGLGL SLVHSIMEHN GGHILLDSRP GEGTRFCLLF RPLDDEALKS IPMHTPVETP
     SLKAGRVLVV DDEPALTEFL KETLELQGLQ VIALNDSREA LDLLLEPEQQ FDLLITDQTM
     PGMLGTELAT QAKNHLGDLK VILCTGHSEQ INADNAAEFG IDSFLKKPIG IQDIVIAIDN
     LSK
//
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