ID A4Y252_SHEPC Unreviewed; 1196 AA.
AC A4Y252;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Precursor;
GN OrderedLocusNames=Sputcn32_0303 {ECO:0000313|EMBL:ABP74035.1};
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP74035.1};
RN [1] {ECO:0000313|EMBL:ABP74035.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 {ECO:0000313|EMBL:ABP74035.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) 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; CP000681; ABP74035.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Y252; -.
DR STRING; 319224.Sputcn32_0303; -.
DR KEGG; spc:Sputcn32_0303; -.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_37_3_6; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd13705; PBP2_BvgS_D1; 1.
DR CDD; cd13707; PBP2_BvgS_D2; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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 Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00062; PBPb; 2.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ABP74035.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:ABP74035.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 529..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 713..934
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 960..1079
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1103..1196
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1009
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1142
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1196 AA; 134956 MW; 4B241D7FCDC3A2A7 CRC64;
MKIILSLIFS LFFMLLASIP LKAKEDVPLT LYGHSTVGEV KLDLSKEQQD WLQQHGKIRV
GITTPDYPPF DMTMDGHSKY YEGLSADYLQ ILSEILKVKI ELHFFDSRPK AIDAIKNNDV
DMLTTANRYE EFYGLELSQH YVEDIPALYI SDKVSPSDTP KRIAIPYDYL PNKQISALFP
DAELVDYPSR LQAVAAAAFG QTDSVIIDAF SANHLINNIF SKQLLLKELL SIDTNGISFA
FNPEKQKLKE IINSALKQIP ISEHWAIKKR WNGGGITVPS KKAYIQFSTD EQTWLAQHKP
IRIVVNEFNA PVSYFDQHRN FQGFAADVLE VISLYSGIET VIIRTQSFEE MEKYLAYDSA
DLAILSPTTR LKNKFTFSKE FTSTPFAVVS HSKTNTLYKQ NITVALPAVH TVNELIPKAM
PNAKVIRVEN YLEAMNAIAK GKVDATIAPL GVADYYINHY YKNILSIDNL VDGIPPAVLA
FAATKDNPQL VSILNKILAS IPPDELQALE NRWRRNAVPG KETWRDYKYT IYTMIAATVM
FILAAIYWTW LTRIHYIRRL DAKQEIQNQL LFMQEVVDSI PHPIYVRDID QQLILCNQSY
QHIFKATNKE DILHKSIEEG SHRVIEAHEL EKEYRKAIQE NRAISRDREI HIDGKAVNIY
HWFQPYKNEH GKICGIVGGW IDVSDRVKLM AQLREAKELA DSASKAKTQF LATMSHEIRT
PMNAIIGLLE LAIKRSHENQ FDFNSIRVAH DSAKGLLALI GDILDIVKIE AGELTLNPTK
IDLKQTISST IQIFEGIALE KKLPLKLIFD HKLPQYVLLD PLRLKQILSN LISNAIKFTN
QGMVTVSAEQ QLELNEQMYL LLKVSDTGIG ISKDDQQKLF RPFAQVQHGA DNKGGTGLGL
AICSSLCDMM GGELRMISEP EQGTTLSMRL PLYPVKDIAN TMLSPSLNVD TDPPTVLPQH
ILIVDDHSAN RLLLSQQLRY LGHSVDEANN GLEAIQLFRQ HPYRIVLTDC NMPIMDGYEF
SRRLRQFEQN NNLPAAVVLG YTANAQLEAK QACIDAGMND CLFKPISLED LRQKLESYCQ
KLTLEHPQQA FLPEALTKLT GGNTPLFEQL LKELLNANEL DLAELQQAVQ QEKLCDAKNI
AHKIKGAAKI VAATSVVSAC EQFEQIKSVD EIEEKLNNLT IAINTLADEI KNHLAA
//
