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Database: UniProt
Entry: A0A1I6Q1C5_9ACTN
LinkDB: A0A1I6Q1C5_9ACTN
Original site: A0A1I6Q1C5_9ACTN 
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
//
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