ID S4MYB6_9ACTN Unreviewed; 1791 AA.
AC S4MYB6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=STAFG_1959 {ECO:0000313|EMBL:EPJ40985.1};
OS Streptomyces afghaniensis 772.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ40985.1, ECO:0000313|Proteomes:UP000015001};
RN [1] {ECO:0000313|EMBL:EPJ40985.1, ECO:0000313|Proteomes:UP000015001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=772 {ECO:0000313|EMBL:EPJ40985.1,
RC ECO:0000313|Proteomes:UP000015001};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA Goodfellow M., Mueller M.;
RT "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT Compounds of the Julimycin B-Complex.";
RL Submitted (FEB-2013) 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:EPJ40985.1}.
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DR EMBL; AOPY01001348; EPJ40985.1; -; Genomic_DNA.
DR PATRIC; fig|1283301.3.peg.1935; -.
DR HOGENOM; CLU_000445_3_0_11; -.
DR Proteomes; UP000015001; 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; 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:EPJ40985.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000015001};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..52
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 92..154
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 194..246
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 286..338
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 378..430
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 470..522
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 562..614
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 654..706
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 746..798
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 838..890
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 930..982
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1022..1074
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1335..1576
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1671..1788
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1640..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1256..1325
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1721
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1791 AA; 192760 MW; A06C56FAF76B0D30 CRC64;
MDTAALNRLM VALVAMRDGN FRKRLTVSGD GVMAEIAAVF NEVADRNLHL TGELSRVRRM
VGREGKLTER LETGACEGSW ATAIDNSNAL VDDLVRPVSE VSRVLSAVAE GDLSPRMELR
TQVPDGNGQP LRGEFLKVGR TVNNLVDQLS TFTDEVTRVA SEVGTEGKLG GQARVRGMSG
SWRDLTDSVN TMAYRLTAQV RDIALVTTAV AKGDLSRKVT VQVAGEMLEL KNTVNTMVDQ
LSAFSSEVTR VAREVGTEGA LGGQAQVPGV AGVWKELTDS VNTMAGNLTA QVRGIAEVTT
AVANGDLSRK VTVPARGEVA QLADTINQMT ETLRIFADEV TRVANEVGAE GQLGGQANVP
GAAGTWKDLT DSVNTVFRNL TTQVRDIAAV TTAVANGDLS QKVTVDVAGE MLELKNTVNT
MVDQLSAFGA EVTRVAREIG VEGELGGQAQ VPGAAGTWKD LTDSVNTAFR NLTGQVRNIA
QVTTAVANGD LSQKVTVDVS GEMLKLKNTV NTMVDQLSSF ADQVTRMARD VGTEGRLGGQ
ARVDGVSGTW KELTDSVNSM AGNLTSQVRN IAQVTTAVAR GDLSQKIDVD ARGEILELKN
TINTMVDQLS AFADQVTRVA REVGTDGRLG GQAQVPGVAG VWRDLTDSVN GMAGNLTAQV
RNIAQVATAV ARGDLSQKIT VDARGEILEL KNTLNTMVDQ LSSFAQEVTR VAREVGTEGI
LGGQAEVQGV SGTWKDLTQS VNGMANNLTI QVRNIAEVTT AVARGDLSKK ITVDAKGEIL
ELVTTVNTMV DQLSSFAEQV TRVAREVGTE GILGGQAHVP GVTGIWKDLS DNVNLMAKNL
TTQVRNISQV SAAVANGDLT RQVTIEARGE VAQLADTINT MVKTLSSFAE QVTKVAREVG
TDGILGGQAH VPGVAGTWKD LTESVNQMAS NLTGQVRNIA MVTTAIAKGD LTKKIDIDAR
GEILELKTTI NTMVDQLSSF AEEVTRVARE VGTEGQLGGQ ARVRDVDGTW RDLTESVNEM
AGNLTRQVRA IARVATAVTR GDLNLKIDVD ASGEIQELQD YINKMIANLR DTTIANKEQD
WLKGNLARIS ALMQGRRDLE DVASLIMSEL TPVVSAQHGA FFLAMPLVDG EDMNASDDDQ
YELRMLGSYG YSMGSMPTSF QPGEALIGTA ATEKRTILVE NAPSGYLRIS SGLGEAPPAQ
VIVLPVLFEG KVLGVIELAS FTPFTQIQKD FLNQIAEMIA TSVNTISVNT KTELLLAQSQ
KLTEQLRERS AELEQRQKAL QASNAELEEK AELLAQQNRD IEVKNTEIEE ARQVLEERAE
QLAVSMRYKS EFLANMSHEL RTPLNSLLIL AKLLADNAEG NLSPKQVEFA ETIHGAGSDL
LQLINDILDL SKVEAGKMDV SPTRIALVQL VDYVEATFRP LTAEKGLDLS VRVSPELPAT
LHTDEQRLLQ VLRNLLSNAV KFTDSGSVEL VIRPARDDVP QKIREQLLET GSLTDPDAEL
IAFSVTDTGI GIASSKMRVI FEAFKQADGT TSRKYGGTGL GLSISREIAQ LLGGEIHAQS
EPGRGSTFTL YLPLHPSELP PQGYQQQLPA LEAGHLMAST SDLSELSEVE VETPAEVKSY
NETQNGPAAL FRRRRRMPEL APRPAQPEQW TPAEQETAPK TQRGIRFGGQ KVLIVDDDIR
NVFALTSVLE QHGLSVLYAE NGREGIEVLE QHDDVAVVLM DIMMPEMDGY ATTTAIRRMP
QFAGLPIIAL TAKAMKGDRE KAIESGASDY VTKPVDPDHL LTVMDQWMRG E
//
