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Database: UniProt
Entry: A0A367FK08_9ACTN
LinkDB: A0A367FK08_9ACTN
Original site: A0A367FK08_9ACTN 
ID   A0A367FK08_9ACTN        Unreviewed;      1388 AA.
AC   A0A367FK08;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-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=DQ384_15950 {ECO:0000313|EMBL:RCG30239.1};
OS   Sphaerisporangium album.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Sphaerisporangium.
OX   NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG30239.1, ECO:0000313|Proteomes:UP000253094};
RN   [1] {ECO:0000313|EMBL:RCG30239.1, ECO:0000313|Proteomes:UP000253094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG30239.1,
RC   ECO:0000313|Proteomes:UP000253094};
RA   Li L.;
RT   "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT   the South China Sea.";
RL   Submitted (JUN-2018) 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   -!- 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:RCG30239.1}.
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DR   EMBL; QOIL01000008; RCG30239.1; -; Genomic_DNA.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000253094; 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; 7.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.1530; -; 4.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; 4.
DR   Pfam; PF18947; HAMP_2; 3.
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; 7.
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; 3.
DR   PROSITE; PS50885; HAMP; 7.
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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000253094};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          106..160
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          200..252
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          292..344
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          384..436
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          476..528
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          568..620
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          660..712
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          965..1197
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1256..1373
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          886..934
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1306
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1388 AA;  150373 MW;  4953427512F948B0 CRC64;
     MKGTPTAEPV PERCYTESEL RPLLETLITW RDGDFRRRVP HAPHGILSEI RLLVNEVADR
     REHLANELLR VRREVVKEGR FGVRLTPGPG VGSWAESVDS VNALIDALVG PVSSAADVLD
     AVAQGDLSRR IDMDRTSRGE VRRLGKAING MVDQLSLFSS EVTRVAREVG SEGQLGGRAN
     LRGMSGSWRD LTEAVNTMSS RVSAQVRDIA VVTTAVARGD LSRKVTVDAV GEMLELKNTV
     NTMVDQLSAF AEEVTRVARE VGTEGELGGQ ARVRGVSGVW KDLTDNVNVM ASNLTSQVRN
     IATVATAVAQ GDLSKKITAD AQGEMLQLKE TLNTMVDQLS MFADEVTRVA REVGTEGQLG
     GRADVKGVSG VWKDLTDNVN SMANNLTYQV RNIAQVTKAV AGGDLSKKID VDAQGEMLEL
     KSTINTMVDQ LSSVASEVSR VAREVGSEGQ LGGQAQVRGV SGVWKDLTDN VNFMANNLTS
     QVRQIAAVSN AVVQGNLSKK ITVDAQGEIL QLKDTVNTMV DQLSMFADEV TRVAREVGTM
     GQLGGQARVR GVSGVWKDLT ESVNELAGNL TYQVRNIGEV TTAVAKGDLS RKIDVDAQGE
     ILVLKTTINR MVDQLSSFAS EVTRVAREVA SDGRLGGQAR VEGVEGTWKQ LTESVNELAG
     NLTTQVRAIA EVTSAVARGD LTRSISVEAQ GELADLKDNI NTMVSNLVAT TKANQEQDWL
     KSNLARVSRL MQGHRDLMEV GKLIMSELTP LVTAHHGAFY MVSSPRDTEL RLIAGYGVRP
     GDGLGPRERF AFGQGIVGQA AAEGRPIVLD NVPSDYLTID SGLSSSTPAQ IVVLPVIFED
     QVLGVMELAS FSRFGEVHLA FLNQLVETIG VTMNTIIANS RTEGLLAESQ RLTTELRERS
     DELQRQQEEL RRSNAELEDK AALLAKQNRA IEIQNFQIEQ ARRTLEERAE QLAVSSRYKT
     EFLANMSHEL RTPLNSLLVL AKLLTENSEG NLTAQQVEFA KTIHGAGSAL LQLINDILDL
     SKVEAGRMDI HPQQISMPKL VEYVEATFGP LAQDKGLSFS VELDPAVPDE LRTDEQRLQQ
     VLRNLLSNAV KFTPKGEVRL DITRAAGVPY IDETLRGSDD ILSFSVIDTG IGIAPEKLDV
     VFEQFRQADG TTSRKYGGTG LGLSICREIA RLLGGEIHAK SEPGRGSTFT LHLPISYSGP
     LANGDGGAAV LDTPQEASLE LTASDVLPEL PAIAEEPPLP HTPVAWQGDD PLNGAKILIV
     DDDIRNVFAL TSVLERHGAT VVYAENGLEG IDQLERNDDV ALVLMDIMMP EMDGWATTST
     IRRMPQFADL PIIALTAKVM HGDREKSIAS GASDYVPKPV DVDRLLERLR GWLTRGRVAS
     GEGREGRG
//
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