ID M7XBC1_9BACT Unreviewed; 1049 AA.
AC M7XBC1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C943_03417 {ECO:0000313|EMBL:EMS34730.1};
OS Mariniradius saccharolyticus AK6.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Mariniradius.
OX NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS34730.1, ECO:0000313|Proteomes:UP000010953};
RN [1] {ECO:0000313|EMBL:EMS34730.1, ECO:0000313|Proteomes:UP000010953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK6 {ECO:0000313|EMBL:EMS34730.1,
RC ECO:0000313|Proteomes:UP000010953};
RA Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.;
RT "Genome assembly of Mariniradius saccharolyticus AK6.";
RL Submitted (JAN-2013) 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:EMS34730.1}.
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DR EMBL; AMZY02000005; EMS34730.1; -; Genomic_DNA.
DR RefSeq; WP_008624374.1; NZ_AMZY02000005.1.
DR AlphaFoldDB; M7XBC1; -.
DR STRING; 1239962.C943_03417; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG1807; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR InParanoid; M7XBC1; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000010953; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
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; IPR031621; HisKA_7TM.
DR InterPro; IPR036641; HPT_dom_sf.
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 PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF16927; HisKA_7TM; 1.
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; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {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:UP000010953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 560..783
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 815..933
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 956..1049
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 866
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 995
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1049 AA; 118186 MW; 243484F731C3A53E CRC64;
MNLQFYFNPF SIPIFFTALV FLFLLRISFS KDFKLDDRYF SLLMLSCFLY SFFYAIELLG
VNADTIRLFY YLEFIGGVFV APFLFLFVLR YSDQTQLINK FLERLLFACS AFFLAMVLTN
ESHGLFYGSV SAQNNGYFLA VELEKGIFHW LYASYNSLLI IAANILLVRM LFSVPDLYKG
QVLIMLFGTL IPWLAYILVV FGNYPFGLDP VPFFLAVSAI VLFWALYKYR LFRTNPIAFK
TIFENISDGI IIFDRLGDVV ALNLTAKKFF QDTGIQSPSN KSDLAKFQDD LSDLVNGTKA
TIEIEDKISE KSYVVYLRTI NGEHPDGDNF QYLIIRDISE QKATEVLIKA NEEKMQHVNQ
DLLRKEKMLT SIAFATKELL SNQDFEIATQ KAITLIGDGA GADRAYLFEN RIDENENILS
SQRFEWSALG VPPEIDNPNL KDLPIGMFGR AAENFLQNNS FHGIVSQMDE DPELKELFQS
QDILSVLLIP IYVEDHFWGF VGFDDCTNER HWSDAETALL ISFADSISNA IERKNMEKNL
IFSMEQAKEA SVAKSEFLAN MSHEIRTPLN GVIGFSDLLM KTNLEDNQKG YLKSIIQSGN
LLLGLINDIL DFSKIEAGKL ELSQEWFNVR DVAAETLKII QPVVDEKKLQ LQLNVNTDVP
KFVQGDLTRI KQILINLLSN AGKFTHEGKI AMEISVDNLR SSATKKALIF SVIDTGIGIS
KEKQQTIFEA FAQEDTSTTR KYGGTGLGLT ICSKLLELMK SKLELETEVG QGSTFFFTLE
LPFAEQIEEP TLEVSPAIIV EREEKETPAS KGTYKVLLVD DNPVNMLLAK SIVKKLLPSS
EISEAYNGAE AVTQYKREVP DIIFMDIQMP EVSGYEATKQ IRVLEQDRHT PIVALTAGTV
KGEYDRCIEA GMDDYLSKPV LVSDIAGMIE KYLGSQPIEE QGEAISSKFD EYKKSDPEFF
RELVEVSISN ISKLKSALQH HFDQGDLKGV KQTGHALKGV GLNLDFQGLV QAAGDAERLT
EITLSTAPLV NATIEEANRI LALLEKEIK
//
