ID A0A328B7M8_9CAUL Unreviewed; 1941 AA.
AC A0A328B7M8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DJ021_14515 {ECO:0000313|EMBL:RAK61834.1};
OS Phenylobacterium hankyongense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1813876 {ECO:0000313|EMBL:RAK61834.1, ECO:0000313|Proteomes:UP000249842};
RN [1] {ECO:0000313|Proteomes:UP000249842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKS-05 {ECO:0000313|Proteomes:UP000249842};
RA Li X.;
RL Submitted (MAY-2018) 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:RAK61834.1}.
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DR EMBL; QFYP01000001; RAK61834.1; -; Genomic_DNA.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000249842; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; 9.
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; -; 6.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 2.
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; 8.
DR Pfam; PF18947; HAMP_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 11.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; 4.
DR PROSITE; PS50885; HAMP; 10.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
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:RAK61834.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000249842};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 102..159
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 199..251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 291..343
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 383..435
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 475..527
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 567..619
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 659..711
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 751..803
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 843..895
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 935..987
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1261..1494
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1542..1655
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1803..1920
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 961..988
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1164..1251
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1591
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1853
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1941 AA; 209314 MW; 0E6E9680969DF5AF CRC64;
MSRRTKAQPS EASVETAELL AALRAFRRGD FSVRLPRGLT GVNGEIAEAF NEVVELNDRM
TKEFERLGET VGRQGKINHR AKLPTAQGSW AASVDAVNTL IADMVHPTAE MARVIGAVAK
GDLSQTMDLE NEERPLRGEF LRIGKVVNTM VGQLGSFASE VTRVAREVGT EGKLGGQAQV
KGVAGTWKDL TDNVNFMAAN LTGQVRNIAE VTTAVANGDL SRKITVDVKG EVLELKNTIN
TMVDQLNAFA SEVTRVAREV GTEGKLGGQA QVKGVAGTWK ELTDNVNLMA GNLTGQVRNI
AEVTTAVARG DLSKKITVDV KGEILELKNT INTMVDQLNA FSSEVTRVAR EVGTEGKLGG
QARVEGVTGA WKDLTDNVNF MAANLTGQVR NIAEVTTAVA NGDLSKKITV DVRGEILELK
NTINVMVDQL NAFASEVTRV AREVGTEGKL GGQANVKGVG GTWKDLTDNV NLMAANLTGQ
VRNIAEVTTA VAMGDLSKKI TVDVRGEILE LKNTINTMVD QLNSFSSEVT RVAREVGTEG
KLGGQAQVKG VAGTWKELTD NVNLMAGNLT GQVRNIAEVT TAVANGDLSK KITVDVKGEI
LELKNTINTM VDQLNAFASE VTRVAREVGT EGKLGGQAQV KGVAGTWKDL TDNVNFMAAN
LTGQVRNIAE VTTAVAMGDL SKKITVDVRG EILELKNTIN TMVDQLNSFA SEVTRVAREV
GTEGKLGGQA QVKGVAGTWK DLTDNVNLMA ANLTGQVRNI ADVTTAVAKG DLSKKITVDV
RGEILELKNT INTMVDQLNS FASEVTRVAR EVGTEGKLGG QAQVPGVAGT WKDLTDNVNM
MAANLTGQVR NIADVVTAVA MGDLKRKLTL DAKGEIAALA DTINGMIETL ATFADQVTNV
AREVGSEGKL GGQARVPGAA GLWRDLTDNV NELAANLTTQ VRAIAEVSTA VTKGDLTRSI
TVEASGEVEE LKNNINEMIR NLKDQTLKNT EQDWLKTNLA RFTRMLQGER DLSTVSNLVL
SELAPLINAQ HAVFYVTDRD DDGQTVLNLA ASYAFNNRKH LASQFKVREG LIGQCAYEKS
RILLTNVPKD YVQISSGLGE APPANIIVLP ALFEGEVKAV IELATFGEFN ETQQQFLDQL
MESIGIVLNT IAANMRTEGL LKQSQLLTSE LQAQQEELKK TNDRLEQQAA SLRQSEELLR
TKQEELQQTN AELQEKAHLL SVQNQQVEAK NREVEQAKIA LEEKAEQLAL TSKYKSEFLA
NMSHELRTPL NSLLILSKLL ADNTPGNLSE KQVEFASNIH DAGTDLLGLI NDILDLSKIE
SGTVTLDISE MSFASLRDQV DRTFSQIAVD KKLDFVVELD PALSRSMYTD DKRLQQIIKN
LLSNAFKFTE RGHVKLKVER AHSGWSLAND HLNTAGQVLA FSVEDSGIGI PEEKQRIIFE
AFQQADGTTS RKYGGTGLGL SISREITRLL GGELRVTSVP GKGSTFTLYL PLNFSPAQAP
SSSRATSMPP LPRPMLMPSA FSEDPVEAVA DDRDTIGSGD SVVLIVEDDP RFASILLSLV
HESGFKGVVT GEGAAAPSLA RRFGPDAIML DIGLPDMDGL ALLDLLKRTP ETRHIPVHVI
SADDQKGLGL SIGAFGFTHK PVEREVVVST LQGVKTFVDK VERRIVLVGA EGEAADVLRQ
CFTQVELVAD LASVLDRPAA DRPDGLMIDA SAVPAPALID QLKQTDGRVA PAVVYVPEDI
DAEDDRRLRL AVFGGLVRLA RTPDQLVEQA SLLLHEPMER MSASTKAKLN QNKHDDSVLS
GRKVVVIDDD IRNIFSLASA LEEYGIELSY AESGRAGLEV LDAKPEVDVV LVDIMMPDMD
GYETIREIRS RPGLSDLPIV AVTAKAMKGD RQKCIQAGAS DYVSKPVDID HLVSVLRVSI
QRADAMKLAS DTVVSLLPQA S
//
