ID A0A316AKW6_9BACT Unreviewed; 1203 AA.
AC A0A316AKW6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CLV98_104272 {ECO:0000313|EMBL:PWJ58413.1};
OS Dyadobacter jejuensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1082580 {ECO:0000313|EMBL:PWJ58413.1, ECO:0000313|Proteomes:UP000245880};
RN [1] {ECO:0000313|EMBL:PWJ58413.1, ECO:0000313|Proteomes:UP000245880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100346 {ECO:0000313|EMBL:PWJ58413.1,
RC ECO:0000313|Proteomes:UP000245880};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:PWJ58413.1}.
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DR EMBL; QGDT01000004; PWJ58413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316AKW6; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000245880; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 3.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000245880};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 44..80
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 84..136
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 137..207
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 504..556
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 557..608
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 628..680
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 698..919
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 946..1067
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1104..1201
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1001
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1143
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1203 AA; 135898 MW; 2A099A839B174614 CRC64;
MELISSHTNW QTMHATLQHL NLIGITITPD FRIKQVSAHT LNKTGWEPEE LIGKSIFDKL
VPHDHEDEIR QMLEEGFLGK RKLEKREIPF LAKKGTVRTF SINSVLIQTD GGTMLGVTLI
GDDITRRTRM ESAITKSNSQ LQDLVDNTSD LIQLVAMDGK FIFVNKAWRE VLGYRVDEIA
SMQMTDIIHP QHLDEVNLQL VDIREGKSNP NFEAVFQSKA GKKIFVRGSV NCRYDNGKPI
AYRCILNDYT EKIRAEKAQN LYYSIANWTI NTPNLYDFYH AIHDELGKII DVKNFFIALY
DPNKSYLYFP YYVDQYFKGN VRFTRRRLGN GLTEYAIASN RPLFLSDTDI EELAKTNSLY
LYGVTPQQLL CVPLRIGDRV TGIIGVKSYD DPKMFSARDL ELLEFISGQV ALAIARKQSE
EELSRYLARL NAIFDSSSHL IWSVNKSMQL TSFNSNYADL IQKQIGIRPT LQVTPEKFGW
RMVGHANRRI LESKYRQALR GEPQYFEFKI NENKGPEMWL EFYLNPIRYA EGVIEEVSGI
ARDITRRKEA ELSLRHSEEL FRGIFENLQD IYCRIDRDGK ITMVSQSILK RLGYLPEEVI
GHHLTEFFAD KKLILAALFR IRRTKSLRNF EISMHRKDGT ERQFMINMLM FVDDKGHTSE
VAILARDITE LKRNELELLK AKEQAEHSLK VKEGFLANMS HEIRTPMNGI IGMIDLLGES
ALNEEQRDFV MTIKRSSETL LNILNDILDL SKIEAGKMVL NEAPLSVNEL LLKLVSLFGQ
AAKNKGNTLT YHIADNVPPF VVADQTRLLQ IMSNLTSNAL KFTEKGSVRV NLSLVSKSED
RVKMKVEVHD SGIGISATDR QILFTSFTQL DNSSKKSFGG TGLGLSISKQ LAALMQGQIG
VESAIGVGST FWFTFEAQET TGALVENNES TENQSIENVL LAANPTILLV DDNAVNRKVA
MEILKKSGCQ VVLAESGFSA IDKVEAKYLD QSGMYDLIFM DIQMPDMDGV QATKEIRKRV
PELPPIVAMT AYSMKEDRER FISQGMDDYL AKPIRAHLLI QKVKELIGFK GQSSSDKSTL
AVQEAPAVPV LDKEIIDQLS NIGGKDLVLS VFEDFVAESG ELVAESLTAY AAGDIATVKS
HLHTLKGSAG TVGVSQVAEI ARDAEWKLKS DDRSSLPQAL PALEEAYKVF LSQYPDLLKK
WLK
//
