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Database: UniProt
Entry: A0A1I1FSX3_9GAMM
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ID   A0A1I1FSX3_9GAMM        Unreviewed;       718 AA.
AC   A0A1I1FSX3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05660443_1087 {ECO:0000313|EMBL:SFC00173.1};
OS   Marinospirillum celere.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinospirillum.
OX   NCBI_TaxID=1122252 {ECO:0000313|EMBL:SFC00173.1, ECO:0000313|Proteomes:UP000199058};
RN   [1] {ECO:0000313|EMBL:SFC00173.1, ECO:0000313|Proteomes:UP000199058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18438 {ECO:0000313|EMBL:SFC00173.1,
RC   ECO:0000313|Proteomes:UP000199058};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOLH01000002; SFC00173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1FSX3; -.
DR   STRING; 1122252.SAMN05660443_1087; -.
DR   OrthoDB; 5555669at2; -.
DR   Proteomes; UP000199058; 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; 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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199058};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          53..274
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          294..415
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          438..557
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          616..717
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         348
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         487
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         655
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   718 AA;  80053 MW;  C31A908ABC1DEE83 CRC64;
     MDPSQAKAKL YKVANAQEPQ ILDTSTQEAL KCLLNELDTA HQASKTKSQF LANMSHEIRT
     PMNGIIGMLD LVLATELEKE QRENLDLARL SAEHLLEIIN HLLDLSKIEA GKLDLQPRVF
     DLPEMLGQTV RSLINRAKVK ELQLQYEMSA NLPRFVYGDP SRLRQMLINL LGNAIKFTQM
     GGVYLKVTCV DLQPTEALID LEVTDTGIGM SAEALRKVFE PFEQVDSESN RQFEGTGLGL
     SIVRQLTEMM GGEVSVTSQL NEGSRFVIRL RLPLPASSEV SPGDEKPLEF NDLRVLVIDD
     EPVNQRMLAA MLSQLGVEQE TATSGPEGLF LLRHACDEQR PFDLVLVDAQ MPGLNGFQVA
     ERIGQDQRFG SIPVVILTTA AETGDAQRCR ALGLAGYLSK PIISTELKAL LSYLIGQKAQ
     SNAAGSKGDP TCFLTGLNIL LVDDNPVNQK VAFKLLEKCQ HQVTRAADGH EALELLAQQS
     YDLVLMDIMM PVMDGLEATR RWRQEEQQRK LPMTPIVAMT ANAMQGDREK CLAEGMQGYI
     PKPVNPLLLY REIDRVIAEY RPETVKEAVV PGEFDDLLDQ AASLLEEAMA DEEPPLQEPA
     SSLFDWQRAV EVLGADESLL VMALETFIDE YPEHQQKLEQ AWQEKDLQSL KQAAHTLKSL
     LATFAAEEPC ALARELEILI RQGADPFTLS KVYEGLQNQL DVLFSQLQKH QEEMREKK
//
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