ID A0A1I6Q1C5_9ACTN Unreviewed; 1868 AA.
AC A0A1I6Q1C5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444716_101858 {ECO:0000313|EMBL:SFS46256.1};
OS Streptomyces harbinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1176198 {ECO:0000313|EMBL:SFS46256.1, ECO:0000313|Proteomes:UP000198873};
RN [1] {ECO:0000313|Proteomes:UP000198873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7047 {ECO:0000313|Proteomes:UP000198873};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR EMBL; FPAB01000001; SFS46256.1; -; Genomic_DNA.
DR STRING; 1176198.SAMN05444716_101858; -.
DR Proteomes; UP000198873; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 10.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 8.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 9.
DR Pfam; PF18947; HAMP_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 12.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 6.
DR PROSITE; PS50885; HAMP; 12.
DR PROSITE; PS50109; HIS_KIN; 1.
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, ECO:0000313|EMBL:SFS46256.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198873};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 30..77
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 117..179
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 219..271
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 311..363
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 403..455
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 495..547
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 587..639
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 679..731
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 771..823
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 863..915
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 955..1007
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1047..1099
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1362..1603
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1748..1865
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1665..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1283..1352
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1798
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1868 AA; 199813 MW; D34A394EDA2CDD1A CRC64;
MSEGAVARAG KSGRGGKSRG SGTVEVDAVA LGRLLSALES MRDGNFRRRL TVAGEGPMAE
LAAVYNEVAD RNLHLTGQLS RVRRVVGREG KLTERMESGV SDGAWAKAID DANELVDDLV
RPMAEVGRVL SAVAVGDLDQ RMELRAPGGN GAARPLRGEF LKVGRTVNSL VTQLSEFTDE
VTRVASQVGT EGKLGGQAHV PGVSGTWKDL TESVNQMVLR LTAQVRDIST VTKAVADGDL
SQKVTVHVEG EMQELKNTVN SMVDQLSSFQ SEVTRVAREV GTEGQLGGQA QVEGVAGVWK
DLTDNVNTMA TNLTAQVRDI ARVTTAVANG DLSQTVRVSA RGEVAQLART VTDMNGTLRN
FADEVTRAAS QIGSEGRLDA QARVHGVAGT WKELTDSVND AFRNLTAQVR DIAEVTTSVA
NGDLSKKVTV DVSGEMLELK TTVNTMVDQL SSFQSEVTRV AREIGHEGAL GGQASVLGVA
GAWKDLTDSV NTAFRNLTAQ VRDISQVTKA VANGDLSQKV TVDVSGEMAE LKNTVNTMVD
QLSSFAEQVT RVATEVGIEG RLGGQARVDG VSGTWRQLTD SVNDMATNLT DQVRGIAQVT
MAVAGGDLSR KITVDARGEI LELKNSMNTM VDQLSMFAAQ VTRVAREVGT EGRLGGQAMV
AGVGGVWRDL TDSVNDMATN LTSQVRGISE VARAVARGDL SRKITVDAQG EILELKDTLN
RMVDQLSSFA EQVTRVAQEV GTEGRLGGQA RVDGVSGTWK DLTQSVNSMA NNLTDQVRGI
AEVMKAVADG DLTKKIMVDA RGEILELVTT VNTMVDQLSS FADQVSGVAR EVGTEGQLGG
QARVRGVSGT WKDLTDNVNV MASNLTMQVR GISDVATAVA NGDLSKKVTI EASGEVAQLA
DTVNKMVTTL SSFADEVTRV AREVGTEGQL GGQASVPGVS GTWRDLTESV NQMATNLTLQ
VRNIADVTTA IARGDLTKKI DINAQGEILE LKSTINTMVD QLSLFADQVI RVAREVGTDG
QLGGQAVVRD VDGSWKDLTD SVNEMAGNLT RQVRGIARVA TAVTRGDHTV RIDTDAAGEI
LALQESVNTM ITNLRDTTKA NDEQNWLKSN LARISALMQG RRDLKDVAGL IMSELAPAVS
AQHGAFYLSM PADAESPVVA GPDDGDGFEL RLIGSYGYAA GAHPTSFRPG DSLIGTAAAE
RRTIMFGPTP EGYLAISSGL GQAPPAQVIV LPVVFEDRVL GVLELATFGE FTVIERDFLN
QMAEMIAGSV NTISVNTRTK MLLDQTQETA DKLRMTRNEL EEQQKALKNS NEELMRKADQ
LARTNRDIEV KNSEIEDARQ VLEERAEQLA LSMKYKSEFL ANMSHELRTP LNSLLILAKL
LADNAEGNLS RKQVEFAETI HGAGSDLLQL INDILDLSKV EAGKMDVSPA RIALVQLVDY
VEASFRPLTA EKNLELSVRV SPELPPTLHT DEQRLLQVLR NLLSNAVKFT DTGSVELVIR
AAGTEVPYEI REQMLANGSI ESADAPLVAF SVSDTGIGIA ASKMRVIFEA FKQADGTTSR
KYGGTGLGLS ISREIARLLG GEIHAASEPG RGSTFTLFLP LHPTELPPPG YRQLTEGAPV
LDSAQTREAI ARKAAERRAL EAARAAEHEV VVEVAPPVAG PAPAPVAGAP AVPALPRARG
SQEQEPGGEE QRTEASSAAE RAAATMTRRF REPAVPEESG AGEGAQAGVP GKEAVRRRRE
FHDFRGRKVL IVDDDVRNVF ALTSVLEQHG LSVLYAENGR EGIEVLESNE DVVLVLMDIM
MPEMDGYATT AAIRRMPQFA GLPIIALTAK AMQGDREKSI ESGASDYVTK PVDTDHLVAV
MEEWIERK
//