ID A0A398D189_9BACL Unreviewed; 718 AA.
AC A0A398D189;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-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=D3H35_01700 {ECO:0000313|EMBL:RIE05261.1};
OS Cohnella faecalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=2315694 {ECO:0000313|EMBL:RIE05261.1, ECO:0000313|Proteomes:UP000266340};
RN [1] {ECO:0000313|EMBL:RIE05261.1, ECO:0000313|Proteomes:UP000266340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2E09-144 {ECO:0000313|EMBL:RIE05261.1,
RC ECO:0000313|Proteomes:UP000266340};
RA Zhu H.;
RT "Cohnella cavernae sp. nov., isolated from a karst cave.";
RL Submitted (SEP-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:RIE05261.1}.
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DR EMBL; QXJM01000014; RIE05261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A398D189; -.
DR Proteomes; UP000266340; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR008979; Galactose-bd-like_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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000266340};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..718
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038370488"
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 488..712
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 436..488
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 718 AA; 79544 MW; ECFEC9B543FDC40C CRC64;
MGCAAGDMTR RWMRFCLLAV LLTTAVVSSA VETAMANAGG ERNADGQIPE ATEGILDLTG
HSLAGDGTVL LNGEWEFYWT RLLEPDDLPV YESRAVGMKF ERVPSIWSAY REDGKALKNR
GYATYRLTVK LDKADAGRTL ALYMPSVATA YKLWINEDLA AASGKVGRSK EEMTARNVPD
VIRFVPKGRE LQFVIQVSNF VQRKGGLWEA LRLGNEEQIS YLRTKSILEE ACILGCLVIM
GLYHIGLYRF RKKDPSPLYF GAICLAVGLR MTVLGQTLLP YLLPDMTWQT AVRIEYMTAI
IAFHLLIRYI HSQYPRECSP AVRWISLIAC AGFGLLVTVA PPSIFTQFML PYQLTVALPT
VLYVLVVYVL AAIRRRDGSL LNGIGSGFFG LTVGGDVLYY NHLIPSGNFI PYGLLGFMFT
QSLNLAGRLS REFGRSEQLA HELVQVNEEL EDKVRDRTAE LRASHDRLER INMELTGLEQ
SRKQLLTAIS HELGTPLTSI QGYVKLMIDG VLPADDRESL QLIYNKTKIL DRIIQDLFEL
SKLEAGQLQF RFGDIRIVPF FRGLAEGYTV QFKKSGLRYE LELGEVDVEA VIAADPVRLE
QVIAIFVTNA EKFTLPGGTI RTSLKPGAMP VTQAPAIRLS VADTGPGIAV NDLPFVFDRF
YRGSPSAGKR EDGAGLGLAI AKQIVEQHGG VIGVESRHGE GSTFYMLLPL RHAEEGAV
//
