ID A0A0Q0V8D2_9SPHI Unreviewed; 1195 AA.
AC A0A0Q0V8D2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AQF98_20865 {ECO:0000313|EMBL:KQB98798.1};
OS Pedobacter sp. Hv1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQB98798.1, ECO:0000313|Proteomes:UP000050543};
RN [1] {ECO:0000313|EMBL:KQB98798.1, ECO:0000313|Proteomes:UP000050543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hv1 {ECO:0000313|EMBL:KQB98798.1,
RC ECO:0000313|Proteomes:UP000050543};
RA Ott B.M., Beka L., Graf J., Rio R.;
RT "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT Medicinal Leech Mucosal Castings.";
RL Submitted (OCT-2015) 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:KQB98798.1}.
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DR EMBL; LLWP01000012; KQB98798.1; -; Genomic_DNA.
DR RefSeq; WP_055133908.1; NZ_LLWP01000012.1.
DR AlphaFoldDB; A0A0Q0V8D2; -.
DR STRING; 1740090.AQF98_20865; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000050543; 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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 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; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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 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; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQB98798.1};
KW 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:UP000050543};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 220..272
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 534..753
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 806..919
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 928..1044
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1074..1191
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 434..510
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 855
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 977
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1124
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1195 AA; 133852 MW; 8F03D97AF65F07D7 CRC64;
MKLSLKSNLR LGLGLSLIIL IISSLASYIS INNLIDSGKL VAHSNIVMSN LDNTISTLKD
AETGQRGYLL TGNKVFLEPY IGAREKVNAL YVVLKEQTKD NPYQQRKLEE LKEILDNRLV
IIDNTIEVKM KNGKVAESVL LDGKVYMDKI RLTIKDMQNE EKRLLGVRTA ELNTLSEYTP
VLIIIAAVLS LLITIFFYRK VTFDFDERVK LQQKLEDINT DTARRIELIQ GIARQISSGD
YKVRLDEVQK DGLGSLSGSL NAMAESLQYS FSLLEDKEWL QSGIAKLNDQ MVGEKEIKIL
ANDMLEHIVA HTKSHVAALY ILEEDRNLYL TGGYALTANE KSHKIANGEG LIGQCLQSDK
MIVLDQIPEG EGTISYATGQ TKPKNVVAFP IHRDGFMIGV IELASLNVYT PRKLDFLNSI
SNNIGIAIHV AQNRKKLQEF LEETQAQAEE LQAQHSELEG LNAELEAQTQ KIQASEEELR
VQQEELLQSN QELEERTSSL EEKNLLIQER NIDIQQKAEQ LAQSTKYKSE FLANMSHELR
TPLNSILLLS KLMADNEELD KEYTEYASVI QSSGQGLLSL IDEILDLSKI EAGKMSLEIA
DVMVDEVIAD MQSLFKPIAK DKGLELVVVT AKDIPAHIST DKMRLEQVLK NLLSNAFKFT
AQGKVSLLLS TDQKYNTLTF KVKDTGIGIA QEKVNLVFEA FQQADGSTRR RFGGTGLGLS
ISKELAKLLG GNISLESEEN VGSEFSLTIP INFTENEAFL EEQLTNIETS SHYVELFPPI
AERFTVEHIP GDVEDDRASI KAEDKVILII EDDTIFAKML LEFTRKRNYK GIVAVRGDVG
IELANRYNPL AILLDIQLPI KDGWQVMEEL KSNPHTRPIP VHIMSSLSVK RESLLKGAVD
FIDKPVALEH MKQIFEKLED ALSRHPKKVL IVEENQQHAK ALSYFLSNSN IHTLVVGNVE
ESIEALKKKE IDCVILDMGV PDKVAYDTLE TIKKSDGLEN LPIIIFTGKS LSKGEETRIK
QYADSIVLKT AHSYQRILDE AGLFLHLVEE KGKQPKALVR DNLGGLNEVL KNKVVLIADD
DVRNIFSLTK ALEQHQMKVL PATDGKDALK VLSENPKVDV VLMDMMMPEL DGYETTRAIR
AMQPYKQLPI LAVTAKAMMG DREKCIAAGA SDYISKPVDV DQLVSLLRVW LYDKV
//
