ID A0A160IR48_9BACI Unreviewed; 918 AA.
AC A0A160IR48;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ABE65_018705 {ECO:0000313|EMBL:ANC78717.1};
OS Fictibacillus phosphorivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC78717.1, ECO:0000313|Proteomes:UP000076623};
RN [1] {ECO:0000313|EMBL:ANC78717.1, ECO:0000313|Proteomes:UP000076623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-29 {ECO:0000313|EMBL:ANC78717.1,
RC ECO:0000313|Proteomes:UP000076623};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a strain
RT toxic to nematodes.";
RL Submitted (APR-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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP015378; ANC78717.1; -; Genomic_DNA.
DR RefSeq; WP_066398315.1; NZ_CP015378.1.
DR AlphaFoldDB; A0A160IR48; -.
DR STRING; 1221500.ABE65_018705; -.
DR KEGG; fpn:ABE65_018705; -.
DR Proteomes; UP000076623; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
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; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ANC78717.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; 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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 509..737
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 799..916
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 426..499
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 849
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 918 AA; 102396 MW; BA79C5DEFDC67602 CRC64;
MNNFRFGIRQ KIITGYIVII ICLIAAILAV TNQLDTMKSE RNFIIQHDFA VRDLTSQIEK
DLLKMETNKR AYIITGDESY LQLYNEASSQ WSKDYNTLNQ LLSDNPSQQK RIAEINENIQ
NWVAVAGDPP IQMKQQNDTA GIAEFFKQDP GKSQTEKVLQ QFDSFRDTEK SLTQKRANDL
NEQNRYLEIG LFSLLAFVVL VSTALAWVIS GSIIKTIKEV VGTIRAMTTG GNLSSRIHVK
SNDEIRDLGE ATNELLNSFE ERDWLQRSVT DVVSKNQGVS SLETLAEIFL SATAQITESS
YGAFYIKEGK DENVRFVKKG AFADTDADVG RASFKLGQGL IGQCALEKRV QVIDRIEGEY
TLISSGLGET KPNSILIAPI VHEDEIVAVI ELASLSSYSN QHISFIEKVL ETFGLTINRV
IDRMEIARLL SESQAMTEEL QAQSEELQTQ SEELQMQSEE LQMINEQLES RSQDAEEKSK
ALEIAKKDLE DKAKQLETGS KYKSEFLANM SHELRTPLNS ILILSEMLAE NGNQSLSDEE
LEFAKVIHSS GQDLLNLIND ILDLSKVEAG KLEIMLSEVN LSEFPSNLER NFTHIADQKN
LNFTINVAPD VPTLLQTDEK RFQQIIKNLL SNAFKFTEKG SVSVSVKKVQ TDVIYNGVDY
WLEVAIKDTG IGIPKEKHEL IFQAFQQGDG ATIRKFGGTG LGLSISSEFA KLLGGRLQLQ
SEEGKGSTFK LLIPSISDES VSVQTFLGAS AEVATALEQA SHSIAVAEPP ITAKIVPTEP
EAEQPSITVD EENVFYGKTV LITDDDNRNI FALKTALEQK GMNILIANNG MECLDVLDAN
KKIDLILMDI MMPEMDGYET MQRIRGTGEH KDLPIIALTA KAMKNDREKC LEAGASDYIS
KPLKLEQLFS VMHVWMTK
//
