ID A0A2T0TP99_9BACT Unreviewed; 1181 AA.
AC A0A2T0TP99;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CLV58_101426 {ECO:0000313|EMBL:PRY47358.1};
OS Spirosoma oryzae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1469603 {ECO:0000313|EMBL:PRY47358.1, ECO:0000313|Proteomes:UP000238375};
RN [1] {ECO:0000313|EMBL:PRY47358.1, ECO:0000313|Proteomes:UP000238375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28354 {ECO:0000313|EMBL:PRY47358.1,
RC ECO:0000313|Proteomes:UP000238375};
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:PRY47358.1}.
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DR EMBL; PVTE01000001; PRY47358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0TP99; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000238375; Unassembled WGS sequence.
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; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
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; 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; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
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; 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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 225..277
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 353..404
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 552..774
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 790..910
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 934..1052
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1090..1181
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 840
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 985
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1129
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1181 AA; 130819 MW; D58B8FE3452AA389 CRC64;
MITTGAVKQE FVTLLSGDIS LFDFSQRYGL HGFIYDNPAD SAYAYVSPAF WTALGYATAL
PPGLLASLLA TDTALATQSE REAVHQVTHQ AGHRVTVRTR TRLLSGPDGS ARRLTACTCL
PTSQSAQPAG ADTPALPTAP LDSLLHTVTS NSLLRTIMDS LPILIYIKDT ESRKLFVNRA
EYMYMGATSA RDIIGKSDYE LYPAESARQS ILEDQLVMNS GIPMLGQETL NARHGHDSCW
FLSSKIPLYD EQGKPAGLLG ISLDITARKQ AELELQRTSD MLERTNQVAR VGGWELNLQT
QDIYFSRITR EIHEVPDDYV PTLETAINFY KEGHSRDTIT KAVATCIEQG TPYALDLQIS
TYTGRELWVR AVGQGKFVDG QCVALIGTFQ DIDEQKRTQR LAQESADMLR KLSDRVPGCL
YLFQSFDDGH IAFPYLSTGA TELFELDLNA TDTVAETLLS RIHPEDMPAL IETSRLSRTT
LTNWNADFRV VLPRQGERWI HADSVPEQLA DSTLWHGYFQ DVTARKHSET ELIRARQHAE
EASRSKSEFL ANMSHEIRTP LNGVIGFTDL LMRTQLDPLQ QEYMSTVYHS ANSLLDVISD
ILDFSKIEAG KLDLSIEKTD LYDIGSQVAD MIKYQAHQKG LEMLLNIAPD VPRYIWTDPV
RLRQILVNLL GNAVKFTEYG EIELRVDVRP GPTADQIAFR FEVQDSGIGI APQHQQKIFD
AFAQADSSTT RRFGGTGLGL TISNKLLSLM GSHLQLTSVE NQGSTFFFDV LFRAEPGEPL
DCAIITGLDR VLIVDDNATN RLIVQNMLNL KGIASDQSSN GIDALEKLKR GPVYDLVLMD
YHMPYMDGIE TIRQIRRTLN YSADQLPIIL LGSSADDAYV EAVCHTLSVQ QHLIKPIKIQ
PFFQALAQIH QPQSLPIPLS APVAPATPLV GEQTVLIVED NSVNMMLASA ILRSVSPTIN
LLTAQNGREG VDVFIRSKPD LILMDIQMPE MNGYEATAAI RALDAGQTVP IIALTAGIMK
SERERCLNAG MNDYITKPVV KDTIARILHQ WLPAPEPVVP APPMPNQPIA TLSMTAHFDE
EELRARVGGD KAFMTELLSE VNDYLAGFPA ELHHHRTRRD WTEVKAVAHK LKGSALNLSF
GILATLASEV EQLASAGEGE ARIVELESEL QAEIELLQTL I
//
