ID A0A1K1X393_9GAMM Unreviewed; 855 AA.
AC A0A1K1X393;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02745752_01673 {ECO:0000313|EMBL:SFX43787.1};
OS Marinospirillum alkaliphilum DSM 21637.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinospirillum.
OX NCBI_TaxID=1122209 {ECO:0000313|EMBL:SFX43787.1, ECO:0000313|Proteomes:UP000182350};
RN [1] {ECO:0000313|EMBL:SFX43787.1, ECO:0000313|Proteomes:UP000182350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21637 {ECO:0000313|EMBL:SFX43787.1,
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; SFX43787.1; -; Genomic_DNA.
DR RefSeq; WP_072325904.1; NZ_FPJW01000005.1.
DR AlphaFoldDB; A0A1K1X393; -.
DR STRING; 1122209.SAMN02745752_01673; -.
DR OrthoDB; 5555669at2; -.
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; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
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; 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 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; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:SFX43787.1};
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 Transferase {ECO:0000313|EMBL:SFX43787.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 195..415
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 433..554
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 574..694
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 761..855
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 487
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 623
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 800
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 855 AA; 93857 MW; AF1D919A70FBA841 CRC64;
MLNPSQETEL LFEISLAIGN SLDTGKMLRE SLSTLMRVLN CSGCAVLEYQ SQPQTQPQSQ
LQMSADAVLP TRLQWQMLQS LPRHFLRQPE DALSHFPGLF LPDSEGCLPA FEASLPLTVE
SAAGAACHAF ALPGVGVLLL KKNASALRPE LQASLQKLMN KLANALLACR YEARLQEKIR
AAEAASLAKS QFLANMSHEI RTPMNGVIGM LDLVMDSSLE REQREHLSLA RLSASQLLEI
INHLLDLSKI EAGKFDLQPE TTDLIELVGA TVKSMAPRAW SRNLQIHYDL PEDLPRYVSV
DATRLRQILI NLLGNAIKFT EWGQVTLTLE YLTAVEPASF RFCIQDTGIG IPADRLQQVF
NPFEQVDAAT NRKYEGTGLG LAITRQLVEM QGGQIAVTSE LGKGSCFCFE LPLLLAEAPE
SLDRIPVDLS QQRVLLVDDE PMNRRVITAM LHNVGVQAEC CSSAPEAIFL IRQAARASQP
FALVLMDAWM PGMDGYLATE KLQQEQLLDS TRLLILTSSA VAGDARRCRE LGIAGYLTKP
LTLSELRRAL QEQLSHCETP LHETTADGVL KGIKVLLAED NPINQRLAIK LLEKKGIHPV
IADNGAKAVS LWQQQDFDLI LMDVMMPEMD GLEATRSIRE QEQKMPGCLP TPIVAMTANA
MQGDRERCLD AGMDGYVSKP VQPQALFDEM NRVLVLQEDL RPAGNTQSLL SLDAMVEALS
DSTLETLMSA PLPGKTEQKN SVMTDTNLYD WALAVDHIGG DEELLLEVLA MFMGGLPEHL
AQLEAAVAES RLQQVAEVAH TLKGLLGTFC ATEAVEAVLA LELAAKQGQN PEALLTQVQE
QLARLQPVLQ QRLDA
//
