ID A0A127W2E0_SPOPS Unreviewed; 1028 AA.
AC A0A127W2E0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AZE41_18335 {ECO:0000313|EMBL:AMQ07740.1};
OS Sporosarcina psychrophila (Bacillus psychrophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ07740.1, ECO:0000313|Proteomes:UP000071057};
RN [1] {ECO:0000313|EMBL:AMQ07740.1, ECO:0000313|Proteomes:UP000071057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ07740.1,
RC ECO:0000313|Proteomes:UP000071057};
RA Yan W.;
RT "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL Submitted (MAR-2016) 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; CP014616; AMQ07740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127W2E0; -.
DR STRING; 1476.AZE41_18335; -.
DR KEGG; spsy:AZE41_18335; -.
DR Proteomes; UP000071057; Chromosome.
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; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 2.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011006; CheY-like_superfamily.
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 InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF06580; His_kinase; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 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; 2.
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}; 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 TRANSMEM 16..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 448..666
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 702..818
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 929..1028
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 751
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1028 AA; 117156 MW; F6CBED9E5DD88653 CRC64;
MTCQTAKTIV MNKKKMIVVV GIFVLILISF RFLWIYYNLT ADYPYAEKGI LDLRDIELTD
KRVITLNGEW DFYNNQLIEP GSLEKHLADD EKIGITVPGD WRKIIPEDEK SSYEYGTYRL
RILLDEQKQL FSLYIKEIRS NATVFINGEK VMELGRVGED SESAKSDFRP VEVSLESYET
EIDLLIHVSN YNPVYPAGIT KTIKFGTSSA IKKSQLVSYL MQFTSVVILL MHSVYTLVIF
LLFGRKKELV FLSLTFLCAA ISILIDDDKL LLYLFPAISW TWWVKLLYLS YASSVFFMLQ
FFKQILMENS IHKTRISIPF KALTVLYLLF VICVLLDYKM MIAPLFRVIM FFIPAIIPFT
LSKVVAQGKA YAIYFLLATI SIASSILWGW IKNHAFSTLP YYPFEIIIGV ILFAIYWFKR
FFQATDESKE LTVKLQKEVK RKDDFLANTS HELRNPLHGI MNITQTIYDS EKDNLTEENK
ENLQILMSVG RRMSMILNDL LDITKLKENG IRLQVKEVDL SSVVSGVFDM LQFLKEGKNI
TFRQTGLETF PKVEADENRL FQILFNLVHN AVKFTNEGEI IVSAETQNDM AVIHVRDTGI
GIDEETMKSV FQPYEQADPK ITAFAGGIGL GLSICDQLVK LHGGSINVKS TVGKGSTFTF
TLQIASQQKR IATNESIRQV IPEIASGDQK TTDQFMKEEL PCILVVDDDP LNLAIVGRML
VAEQFDVVTC TSGKEALVLL DKGRWDLVIS DVMMPNMSGY ELTQKIRERF PISELPILLL
TARSQLEDIQ TGFHCGASDY VTKPVEKLEL VTRVKALTDL KTSIGERVRM EAAWLQAQIQ
PHFLFNTLNT IAALSEIDPP KMVELLDKFG NYLRASFASH NLNQVIQLET ELELVRSYLF
IEQERFGDRL NVEWEMRGIP AIQIPPLSIQ TIVENAIQHG VLKRPEGGTV QIRVLEQKDF
IEIIIMDDGV GIPEEKLKSL LNYHTEEQRG IGLLNTDKRL KQQFGSGIDI TSVLNRGTTV
TFIVPKKE
//
