ID C9Z564_STRSW Unreviewed; 1304 AA.
AC C9Z564;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=SCAB_26691 {ECO:0000313|EMBL:CBG69773.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69773.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG69773.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG69773.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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};
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DR EMBL; FN554889; CBG69773.1; -; Genomic_DNA.
DR RefSeq; WP_013000458.1; NC_013929.1.
DR STRING; 680198.SCAB_26691; -.
DR GeneID; 24307983; -.
DR KEGG; scb:SCAB_26691; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_002554_0_1_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR013587; Nitrate/nitrite_sensing.
DR InterPro; IPR010910; Nitrate/nitrite_sensing_bac.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08376; NIT; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50906; NIT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CBG69773.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 394..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..386
FT /note="NIT"
FT /evidence="ECO:0000259|PROSITE:PS50906"
FT DOMAIN 417..487
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 604..710
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1304 AA; 134931 MW; 081E6C15E2CC67FC CRC64;
MQGRFKRDGS ASAEPEPHNG TGNGSSPQHA QNPGPAEIGD GGERSGRPGA SAAPQQSGKP
KGGTTGGGTS GSRVALRNWR ISTRLVSLLA LPVVAATSLG ALRIGDNVDD IQQLDNMRLL
TDMTKQATEL ATALQNERDE SAGPLAHGVN AGDYTIKGVR EKTDLARTQF TDATQAAETA
TTTEKMPGVR DSLVRVVREL YNLSSIRKNA YVDPKNSTQT VEAYHRLIDQ LLELSTDMAE
ATSNPDMIKR TRALAAFSSA KEYASVQRAV IAAALPDSDD KAGKLSENDR LYANAALANE
ESDRSTFSDI YGGGAEDVTK PIDDASPTVE ASDVYADRVL GSASGLGGQD KRSYRDWIDD
SGAKIERMKK IEGSLLEEME QTARNLRADA EQEAIISGAL ILLVLGVSLV GAFVVARSMI
RSLRRLQDTA TKVAQDRLPE LVKQLSESDP QDVDTSVESV GVHSRDEIGQ VAAAFDDVHR
EAVRLAAEQA LLRGNVNAMF TNLSRRSQGL IQRQLSLISE LESREADPDQ LSSLFKLDHL
ATRMRRNGEN LLVLAGEEPG RRWTRPVPLV DVLRAAASEV EQYERIELAS VPTTEVAGRV
VNDLVHLLAE LLENATSFSS PQTKVKVTGH ALPDGRVLIE IHDTGIGLSP EDLAAINERL
ASPPTVDVSV SRRMGLFVVG RLSQRHGIRI QLRPSDSGGT TALVMLPVDV AQGNKKPTPG
KPGQGGPSTG GPAAAQASAG AAAARRQAGN PSGAPLGGPS AGGGLLGGPP QRGQVGAGQG
PRAALPGNPS GPGGLGNPGG PRGPQGGPPV PPQGGRPPAG AGAGGFGNGG AFGGGQAPGA
PQGLQAAGTG GPNGFESFDD SGRQGGFPTG SGLRPAGGPG DAGASRPGGA DGGPGAVPPK
QGKERSGRRR PQLPGRGGPR AELPGGNTSS RTPSWSDDNA QPPVPRASLD APRGHEEQPD
VTAPMPRVAP GQTPGSPADF PHSTGADFDS RRPGAGTPAP DGTGSYVRSD VYGGTGAPPA
PTGPSRGASQ DPSSTGQFAA TGYDASGTGQ FPAPGRPNPQ GAGQYGAPGR PGPQDPGQYG
VPGGQNGQGP GRYDTPGRQN SQDTGQFERP QVNGSFDAPR QPVPPQRPPV PPQRPARPQE
PEALPPATGP MDGRTPLYDT LETNWFHGQG GQNGRPGNGS APQQAAAPAP QTPAAPQRPA
APAAPASTTW RSTPNDDLVR QAERARQPSA GGVTTSGLPR RVPRANLVPG TAQQQQHQTG
PQVSRSPDDV RGRLTNLRRG IAQGRQAGNG QTGSFPSPTH QQER
//
