ID A0A1I0ELV3_9BACL Unreviewed; 1082 AA.
AC A0A1I0ELV3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN03159358_1756 {ECO:0000313|EMBL:SET46367.1};
OS Paenibacillus sp. NFR01.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566279 {ECO:0000313|EMBL:SET46367.1, ECO:0000313|Proteomes:UP000198735};
RN [1] {ECO:0000313|EMBL:SET46367.1, ECO:0000313|Proteomes:UP000198735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFR01 {ECO:0000313|EMBL:SET46367.1,
RC ECO:0000313|Proteomes:UP000198735};
RA de Groot N.N.;
RL Submitted (OCT-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; FOIK01000001; SET46367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0ELV3; -.
DR STRING; 1566279.SAMN03159358_1756; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000198735; Unassembled WGS sequence.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 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 Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000198735};
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 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 290..344
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 365..417
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 718..933
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 955..1069
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 37..64
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 256..290
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1004
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1082 AA; 123460 MW; 97F7577FDD27525C CRC64;
MKRRKLSDVS IKTKYSRIIF SLLVLVILIG VGLFAYINSE QRRLDNEREM LQQKAETVDK
LAESLNDVLF RGRGYIAFKS DSELQQLYAA LDQLDVDTAA YGLLNLSREE AEYRDELTSF
AAKYRNELLP QVIGLVQSSD EEGILKFSQA GNTDAVNSIL AYTQQFRKDT LEQVNGITAD
SIREANLLSV VAFSISAVLL LIFTFLIWRI LQILIGPILK LEEASNSLAA GEAVLLGNLD
KRDEIGRLYE AFLNMARNIQ DKEEELTMQN EELVAQQDEL QDQQFRLERS LSEIESMMKA
LDQSSAVATF SNMGVFTHVN DNFIDYTGYT GSEILGNTYR LLSIQNFSEE QIREIGRRLS
TGGVWSNEVE VKTKDGAAVW MHMSMMPYLN DEGQVYKYIL IANNISYLKQ VQRELAATLV
QTEQTKIMLE RSNQLNHDIT YTLDKQEFAE KFIAFMNKQY QFDSTMFFFV KDRTFFSKGV
PQENLDRYLR SENGNMLYRM QTERSYITKR LASEREQGIA PEGTYAYDYY SSVLNGEGEI
LAVFAATRIG QSYSEEETDE IRGLMNRVAL AIERLQMYQE IEDGRKLNRD IVNNVNEGIQ
FVQSDGRMLH INKALSQMFD FGERDEGEEL PKEEWLEHFL EHSNESLELR QFYGQMLSTA
TSESGTLKYS LGKDNKRHID VYAIPVYRRE VRFGTLFVHR DITREFELDL MKSELVSTVS
HELRTPLSSV LGFTELLLAK TMKPEKQLKY LETIHREAKR LTDLINDFLD LQRMESGTQT
YNSERVNLSE LVLGVIDQFK MSSTTHHILL ADEAQNAKVE IDRDKIVQVL TNLLSNAIKF
SPGQNEVNVQ LYNEGSRIVV EVQDHGLGIP KEQIGQLFQK FRRVDNSASK RIGGTGLGLA
ICKEIMDKQK GTIGIESVEG EGTVVRFTLP VEYTEGSRHE DEPQRTGADK ELKPEVMIVE
DDYSLSLLLS EELKGKGFRV THHYHPVQAF EQAVKTPFVA IVVDLMLGEE LDGWDLIRML
KDDPRTENIP IVISSALDKG DKELMESVRN YLTKPYPPGE LTTALQQIVA ARSANGDVLF
PE
//
