ID A0A1K1X0R7_9GAMM Unreviewed; 1341 AA.
AC A0A1K1X0R7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02745752_01639 {ECO:0000313|EMBL:SFX43111.1};
OS Marinospirillum alkaliphilum DSM 21637.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinospirillum.
OX NCBI_TaxID=1122209 {ECO:0000313|EMBL:SFX43111.1, ECO:0000313|Proteomes:UP000182350};
RN [1] {ECO:0000313|EMBL:SFX43111.1, ECO:0000313|Proteomes:UP000182350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21637 {ECO:0000313|EMBL:SFX43111.1,
RC ECO:0000313|Proteomes:UP000182350};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FPJW01000005; SFX43111.1; -; Genomic_DNA.
DR RefSeq; WP_072325874.1; NZ_FPJW01000005.1.
DR STRING; 1122209.SAMN02745752_01639; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000182350; Unassembled WGS sequence.
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; cd00130; PAS; 4.
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; -; 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; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029016; GAF-like_dom_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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
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 NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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; SSF55781; GAF domain-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; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000182350};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 16..85
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 95..146
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 147..219
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 222..275
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 276..347
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 351..403
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 586..631
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 663..714
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 732..954
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 980..1094
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1132..1231
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1029
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1178
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1341 AA; 150143 MW; 7EEEFD138FAD6A17 CRC64;
MKNQPVIHRH YDLGKQQELL NQLAENTPGV LYQYRLFSDG RSCFSYATQG MLDVYGFTPE
QVAEDARPVL ERLHPDDLEQ VNQSIILSAA TLQVWEADYR YLHPKKGERW MEGRATPARL
DDGSIIWNGY IYDITDRKLQ ELHLQDLSTR FQLTMEATDT GLWSWDLTTN EVSWSSQAFR
QLGYEPDAFP VSLDKFQQLM HPDDTRPMMS EVMHCLEQVK GFEVQFRLKH AAGHWVWIQG
RGKVTELSVE GKPIFMMGTH INISSLKQKE AELRESEQRL SQLAAYSRTV TWEMDAKGLY
TYVSPVCRDV WGYDPDELIG QKHFYELHPI EDREHFIEQA FTIIAAGQSI NDFENPVLHK
DGHLLWVTTN GFPILDTNGL LIGYQGSDRD ITQQKNAELG TRQLEAKISR QRHALDQIAL
AIAKHQDVDG ILDAVCQHMG QALQADRALV YDVNFEKQLI HGLQEWLNPD LPKLTSSIGT
YPLAVFEAGV TLMRHQQQWL VSHQSQPHPV LMQDGSAEVL HQQMAIKTLC WLPFRFTDQG
YQLLVFNWVA EPIALAAEEQ AFLGSIARMV ELALGKIQML EASQTQQKRI QFVYDVMGEG
FYTLNEQGLI TDINPAACRM LGYQKDELIG KIGHDIFHAH VGNQHLPLQQ CPIFSTIRKG
QVFNGEETFQ CKDGRIIVVQ VVSAPLFESN GSKVSVTSFT DITERKRAET AILEAKAAAD
AANRAKSEFL ANMSHEIRTP MNGIIGLSQL SVNEHSHDVL QDRLYKINQS GRTLLGIIND
ILDFSKIEAG KLSIDLQPFF LPSLLDNLNS LFTQMASEKG LILKISARSL SHNAWIGDEL
RLRQVLTNLL GNAIKFTDQG QVDLLVSQQF DKDGKQTLLF QIQDTGIGIT PDQQQKLFKA
FSQADSSITR QHGGSGLGLV ISQRLVNAMG GQGIQLVSHL GVGSSFSFTL PLQPCSSAEE
QLLSNQHHQL HDTLLQLKGR LLLVEDNPIN QEVAQAQLQQ MGMEVVLAEN GAEALTRLSQ
QTFDLVLMDI QMPVMDGYEA TRQLRQAGHT LPVIALTAAA MIEDQQKALA SGMNDHLAKP
IDTHALQQVL ARWLTADTAS DRPSPTPVVP AESTTQPAFL DTTAGLVMLG GNNTLYNKLL
GQFLEQLEAD YLPLVLQLQQ LQPDSPPEAY ATAQKKAHTL KGVAGYLALK HLAHCATELD
LRLKQAQQPP ESMILAFATS LKQTRDAINT HRLHNGSASP AMETTAVTVE SSDPQATETQ
QPTLAETLLA LQKAIHNNMY LDDQLLEAMG KQFPESQQHP WQQLIRALDG FHYAQAEQLL
ISIMQQLEHP PANTTVMSKQ P
//
