ID A0A1T4WNL1_9CLOT Unreviewed; 764 AA.
AC A0A1T4WNL1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05428976_103175 {ECO:0000313|EMBL:SKA78933.1};
OS Clostridium sp. USBA 49.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1881060 {ECO:0000313|EMBL:SKA78933.1, ECO:0000313|Proteomes:UP000190748};
RN [1] {ECO:0000313|EMBL:SKA78933.1, ECO:0000313|Proteomes:UP000190748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 49 {ECO:0000313|EMBL:SKA78933.1,
RC ECO:0000313|Proteomes:UP000190748};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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};
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DR EMBL; FUYD01000003; SKA78933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4WNL1; -.
DR STRING; 1881060.SAMN05428976_103175; -.
DR OrthoDB; 9784397at2; -.
DR Proteomes; UP000190748; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR033425; MASE3.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF17159; MASE3; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000190748};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 18..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 280..316
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 406..466
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 474..526
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 539..749
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 764 AA; 88004 MW; 0DCB7505BEC7754C CRC64;
MDATFKIKET FTNLNKNALV NILLSLFLSF IVALIIHSSF IKQLDIYYMI LEMICIFITL
SLFVSIWYSS KYNISILSFG LLISAIFEVF RCCYLLKSNL NIYYSINLSN KFWIISRFTQ
AVFMFFYAKN LKIIINKWIG LIIFVFLTAS ITYFSIFSSE YLLAIFTYNG IKVLEIFFKY
AIIILFLLTA YNIKNKNKKF ANTKHIYVYN CIVLAIVSEI CFIYYRNYSS IIYSMGCTLK
TISYYFLFKA IFVNTFIFSF SKLKKEHKIL EEAVYEVNSI TQTLSDILEA LPFAVFTYND
EGRIKYINSK FEEIFNCNRI NLYNLTTFEL SKIFKNINTE EKTLWDIVSQ SEGNEIKMFR
TYKLQNGEYK KVAITSRKIK GGVIALIKEA KEEQVLSNLN LQTETILNSV SNSVLMIDKD
KKVVLCNRAF EELAEIKKED IIGIDIDKLS EMIHYEGGKL IKDALQGQCI DHDKFKEISL
TTLDGDVKEI SIYTGNIKNV EGEIIGAISI NTDITEIKKE QFKIRQQEKL AILGQLGAGI
VHETRNFLTN IKGRCQIIEA ISKDESIKKY ASKINNDVDE VNSIISEFLF LSKPRETQMQ
EVSMVDIFQS IKNLVETSSL VKGVNVNVFL SEEERYLLCD EVQIKQVILN ICKNAVDAMT
YKENAVLNIE TGYDEDKNEM FIKISDNGKG MSEEEIKKLG TIFYTTKNNG TGLGLNVCYQ
IINEHNGRIE VESKPMEGST FKIILPCIED TYEDEDIENS TLIK
//
