ID A0A1M7R0M5_9BURK Unreviewed; 1809 AA.
AC A0A1M7R0M5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05192549_10961 {ECO:0000313|EMBL:SHN38129.1};
OS Duganella sacchari.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=551987 {ECO:0000313|EMBL:SHN38129.1, ECO:0000313|Proteomes:UP000184339};
RN [1] {ECO:0000313|EMBL:SHN38129.1, ECO:0000313|Proteomes:UP000184339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sac-22 {ECO:0000313|EMBL:SHN38129.1,
RC ECO:0000313|Proteomes:UP000184339};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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: 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}.
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DR EMBL; FRCX01000009; SHN38129.1; -; Genomic_DNA.
DR STRING; 551987.SAMN05192549_10961; -.
DR Proteomes; UP000184339; 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 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; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR013785; Aldolase_TIM.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
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 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR45339:SF3; HISTIDINE KINASE; 1.
DR PANTHER; PTHR45339; 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; PF07494; Reg_prop; 7.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 2.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SHN38129.1};
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}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1122..1344
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1364..1486
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1535..1634
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1559..1692
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 833..881
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1053..1115
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1413
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1574
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1625
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1809 AA; 200094 MW; 4E08048810AF63A3 CRC64;
MLLWESTALA GAPPRTLRFE QLSVEHGLAQ ETVLAIAQDK QGFIWLGTQA GLTRFDGYRT
VTYKSAISEP RSLADNWVRV LHLDRSGQLW VGTDGGLDRY DAATKTFTHF LPHESAQRGN
GNRHVRAIAD DGLGGLWVAT ADGLHHFDPN SKRFNSWHHD PADAGSLASD HVTSLARDAA
GRLWVGTASG LDMLPAGGTR FQHYTIDASG DSKFNSVNAL QVDEAQTLWV GTQGGLEQWR
LLGAEPQRRR LGAREGLKPG TSITALYEDA ENNVWAGSLA DGLFRWLPSE GRLVQYRHQV
SDTHSVADNQ ISALFRDRVG TFWVGTWNDG ASRVDMGSGG FARIVRQADQ PNSLSDNKIR
SILPDGHGKL WLGSSGGLNL YDAVTGESKV WRHNPQNPNS ISDDQITTLW REKNGNLWIG
GQAGINHLNL NSGAIRSISF VRGDPASDTI RNIVGDRNGV LWVASRGGLH RLDPVTMETR
TFRHDPSDSG SLSDNVVRPI LEDRRGQLWI GTFNGLDLLD RKTGKFRHFR RDAVNQNSLS
HDEVHCLYED ALGTIWVGTA AGLNKMEVAA DGSVKFRRYL RKDGIADDAI ASILPDDAGN
LWLSTNSGLS RLNIETGLVR NYSGADGTIE GAYFDGAALR TPDGILYFGG FNGITAFAPS
EVRENSVAPT VAITDFQIFN KSLKPGQGEH GDVLRTAIEH TAALTLLEGD SVFSLEFAAL
HYAAPQRNRF AYQLQGFDED WVVTDSTKRF ATYTNLDPGK YVFRVKAANK DGIWNDNAAT
LEITIKPPFW KTWWFRSMLA LIAAGGAYAV YHARVRALRH QQLRLEHLVG SRTAEVEYKN
QQLQHQKHEL ERRRLEAEAQ RAEAEQRRID TERQKEEVEQ AHRNISVLSE LGREMSASLD
METTMQTLYR HVNHLMNAQI FGIGFVLEEE GVIDFPFAIE GGVRTYPYQR RLDQPDQLAV
WCLTHRKPIF INDFLKEYRD YMSESGLESL VPCEREDGMP VATAHSMMYT PLIIGDKVVG
LLCVQSTERN AYQRIHMDML QTLAAHAAAG LENARAYQEL EETLQTLRQT RDQLMAQERQ
VRHHTEELAR TNRALQDNEE RLRYAKQKAE DATRQKSEFL ANMSHEMRTP LAGVIGMLGF
ALRDPQLAAS TREQIMRGQA NAQSLLSIIN DLLDFSKIEA GKLTIENIDF SLSGAVENVV
GLFEEQAAAH SVGFSLEFSD DLPQFVVGDP TRLRQVLVNL VGNAFKFTLH GSVRMRVERA
PDDGTENRIR FSVSDTGIGI EADAIPRLFQ QFEQADASTT RRYGGTGLGL AICRQLVELM
GGSINAVSTP GEGSTFMFEL PLPNGVAPPV VPHVPREPHS HQLKVLCAED FPTNQIIIRM
MLEDLGHKVD IAANGALAVK ACSLTRYDLI LMDGRMPEMD GASATRLIRS GGPDVAPVRD
QELMIIALTA NASEEDRSRY LASGMDDFLT KPIDEDKLHF QLSRAIERQL QRGFQLPRMQ
PRRNPAIGTP ELDSMFGVAP ASLETSRLAQ HSGGPSDLKA RLRQAFNQDA PLRLADLEHA
LAQRDREAAG RLLHGLKGSA GYLEEQELQA LCGDLEMEAD HGNWPQVESA MPHLDGLRPA
ICFCDLRMPR LSGMELLQRV KGHPEINTMP FVLVTSANDK DTVLEATKSG AAGYIVKPFQ
AEQVRVHLVN FLDQAANGYD HHAETPTDTL RRLGINAERL LVYLSGFQNQ LTAAAGDLQT
MLANGEQPEA QVRIDRLHAG CVTLGLHGAA AALKGIGPGQ LSNDVVQAVL SDVVRAVIHQ
SGLVRQESV
//
