ID A0A086MWU2_9ACTN Unreviewed; 1825 AA.
AC A0A086MWU2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=FM21_21325 {ECO:0000313|EMBL:KFG73360.1};
OS Streptomyces mutabilis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67332 {ECO:0000313|EMBL:KFG73360.1, ECO:0000313|Proteomes:UP000029095};
RN [1] {ECO:0000313|EMBL:KFG73360.1, ECO:0000313|Proteomes:UP000029095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRM45540 {ECO:0000313|EMBL:KFG73360.1,
RC ECO:0000313|Proteomes:UP000029095};
RA Luo X., Zhang L.;
RT "Complete genome sequence of the Streptomyces mutabilis TRM45540.";
RL Submitted (MAY-2014) 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:KFG73360.1}.
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DR EMBL; JNFQ01000002; KFG73360.1; -; Genomic_DNA.
DR RefSeq; WP_043379192.1; NZ_KN039947.1.
DR STRING; 1915400.FM21_21325; -.
DR HOGENOM; CLU_000445_3_0_11; -.
DR Proteomes; UP000029095; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 11.
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; -; 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; 10.
DR Pfam; PF18947; HAMP_2; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 5.
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:KFG73360.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..84
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 124..186
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 226..278
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 318..370
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 410..462
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 502..554
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 594..646
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 686..738
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 778..830
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 870..922
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 962..1014
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1054..1106
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1367..1608
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1705..1822
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1288..1357
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1755
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1825 AA; 195255 MW; 23D2D422DFFBB6A4 CRC64;
MESGAATRGT KARAKGGQSL SNQGRSRGGS TTVDTAALNR LLAALVAMRE GNFRKRLTVS
GDGVMSEIAA VFNEVADRNL HLTGELARVR RVVGREGKLT ERLETGACEG SWAAAIDNSN
ALVDDLVRPV SEVSRVLSAV ADGDLSPRMD LRTQTAEGTG QPLRGEFLKV GRTVNNLVDQ
LSTFTDEVTR VASEVGTEGK LGGQARVRGM SGSWKDLTDS VNTMAYRLTA QVRDIALVTT
AVAKGDLSRK VTVHVAGEML ELKNTVNTMV DQLSAFSSEV TRVAREVGTE GALGGQAQVP
GVAGVWKELT DSVNTMAGNL TAQVREISHV TTAVANGDLS KKVTVPARGE VAQLAETINQ
MTETLRIFAD EVTRVANETG GEGQLGGQAN VPGAAGIWKD LTDSVNTVFR NLTTQVRDIA
AVTTAVASGD LSQKVTVDVA GEMLELKNTV NTMVDQLSAF GAEVTRVARE VGVEGELGGQ
AQVPGAAGTW KDLTDSVNTA FRNLTGQVRN IAQVTTAVAN GDLSQKVTVD VSGEMLQLKN
TVNTMVDQLS SFADQVTRMA RDVGTEGRLG GQARVDGVSG TWKELTDSVN SMASNLTGQV
RNIAQVTTAV ARGDLSQKID VDARGEILEL KNTINTMVDQ LSSFAEQVTR VAREVGTEGR
LGGQAQVPGV AGVWRDLTDS VNGMAGNLTA QVRNIAQVAT AVARGDLSQK ITVDARGEIL
ELKNTLNTMV DQLSSFAQEV TRVAREVGTE GILGGQAEVQ GVSGTWKDLT QSVNGMANNL
TMQVRNIAEV TTAVAKGDLS KKITVDAKGE ILELVTTVNT MVDQLSSFAE QVTRVAREVG
TEGILGGQAH VPGVVGIWKD LSDNVNLMAK NLTVQVRNIS QVAAAVANGD LTRTVTIEAR
GEVAQLADTF NTMVKTLSSF ADQVTKVARE VGTDGILGGQ AHVPGVAGTW KDLTESVNQM
ASNLTGQVRN IAMVTTAIAK GDLTKKIDID ARGEILELKT TINTMVDQLS SFAEEVTRVA
REVGTEGQLG GQARVRDVDG TWRDLTESVN EMAGNLTRQV RAIARVATAV TRGDLNLKID
VDASGEIQEL QDYINKMIAN LRDTTIANKE QDWLKGNLAR ISGLMQGRRD LQDVASLIMS
ELTPVVSAQH GAFFLAMPHA DGQEHAGADG DQYELRMLGS YGYSMGSMPT SFRPGEALVG
TAAQEKRTIL VENAPSGYLK ISSGLGEAPP AQVIVLPVLF EGQVLGVIEL ASFTPFTQIQ
KDFLNQIAEM IATSVNTISV NTKTEVLLKQ SQELTEQLRE RSEELEQRQK ALQSSNAELE
EKAELLAQQN RDIEVKNTEI EEARQVLEER AEQLAVSMRY KSEFLANMSH ELRTPLNSLL
ILAKLLADNA DANLSPKQVE FAETIHGAGS DLLQLINDIL DLSKVEAGKM DVSPTRIALV
QLVDYVEATF RPLTAEKGLD LSVRVSPELP ATLHTDEQRL LQVLRNLLSN AVKFTDSGAV
ELVIRPARDD VPQAIREQLL EAGSMTEPDA QLIAFSVSDT GIGIAASKMR VIFEAFKQAD
GTTSRKYGGT GLGLSISREI AQLLGGEIHA QSEPGRGSTF TLYLPLHPSE LPAHGYQQPL
PALEPGGVLA TPGAGIALPG PQTERPAEVE SYHDSRSGAA ALFRRRRRAA SETEEGPGSQ
LEQQPPAERD ASPQSSRGIR FGGQKVLIVD DDIRNVFALT SVLEQHGLSV LYAENGREGI
EVLEQHEDVA VVLMDIMMPE MDGYATTTAI RRMPQFAGLP IIALTAKAMK GDREKAIESG
ASDYVTKPVD PDHLLTVMQQ WMRGA
//
