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Database: UniProt
Entry: A0A1S1Y7J5_9GAMM
LinkDB: A0A1S1Y7J5_9GAMM
Original site: A0A1S1Y7J5_9GAMM 
ID   A0A1S1Y7J5_9GAMM        Unreviewed;       908 AA.
AC   A0A1S1Y7J5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=BJL95_21645 {ECO:0000313|EMBL:OHX37268.1};
OS   Methylomonas sp. LWB.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=1905845 {ECO:0000313|EMBL:OHX37268.1, ECO:0000313|Proteomes:UP000180009};
RN   [1] {ECO:0000313|EMBL:OHX37268.1, ECO:0000313|Proteomes:UP000180009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LWB {ECO:0000313|EMBL:OHX37268.1,
RC   ECO:0000313|Proteomes:UP000180009};
RA   Stephenson J., Kumaresan D., Hillebrand-Voiculescu A.M., Murrell J.C.;
RT   "Draft genome sequence of the methane oxidising bacterium Candidatus
RT   Methylomonas sp. LWB isolated from Movile Cave.";
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OHX37268.1}.
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DR   EMBL; MKMC01000012; OHX37268.1; -; Genomic_DNA.
DR   RefSeq; WP_071156913.1; NZ_MKMC01000012.1.
DR   AlphaFoldDB; A0A1S1Y7J5; -.
DR   Proteomes; UP000180009; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 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; 6.10.340.10; -; 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   InterPro; IPR033417; CHASE8.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
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; PF17152; CHASE8; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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; SSF158472; HAMP 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   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
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   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OHX37268.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000180009};
KW   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        15..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          189..242
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          282..507
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          659..778
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          812..908
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   REGION          777..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         708
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         851
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   908 AA;  99699 MW;  C29A74D49B006B20 CRC64;
     MARRKLPDLP MKQKLLYLQE LTVALALLFT LPITSLTQIH QERSRLETET RSLSTMVGFS
     ASAALLFDDV KTANGVLATL RGKPEILSAQ LYSREGLLFA QYPSSDTTPD VPRDLSDARL
     EIASNGWRLT EQVLIYPVSG EGPEIIGHLR MAVDLRPMWR TVLINMAQLF GALLTAVVLA
     VLFGRNLAKS IAAPLTALSS LARKVSQDND YMVRAGGGGD DEVGQLVASF NSMIERLQQR
     DAELAKQREN LERQVDLRTV DLRRAVAEAQ AANLAKSQFL ATMSHEIRTP MNGVLGMTEL
     LLGTRLDDTQ RQYAETVFSS AESLLTIIND ILDFSKIEAG KLQLETIDFS LYELIEQLSA
     LFWERARAKH IELDCRIDAS VADAVRGDPH RLRQILTNLL SNAIKFTERG SVGLYVSAAE
     ADPAAPERRL PLVFRVVDSG IGIAEEILPK LFKPFNQADG STTRKYGGTG LGLAICKELS
     SLMDGRIEVR SQLGVGSQFA VYLPLAPAGA LLPPVNVDPI LRGRRALVVA NGQLDIECLC
     LELSELGVHF KLAANEASAL LRLEEGAKSG IYYDFILFDV ATLDVGVLNE RLQTLPRLAS
     IRAVEISGAS GPDPKRPLPD WPVLYQPIQR QALREVLLLG VDGKPSIADL VAVRCDRRRI
     LLAEDNPVNQ KVAKAMLDQL GYRVRIADNG KSALHIYESE PIDLILMDCM MPEMDGYSAA
     RLIRDSERQQ GGTRIPIIAL TANAMEGDQQ KCLDAGMDDY VSKPFLQQAL ASKIGRFLPH
     SGNNESPARP PIDKDLDKLD NNALDTLRQI GGDQLVTEVV DLFRQNALEQ IDLIATGLRE
     QNPQAVRFAA HALKSAAANI GARGLSEQAK AIEHAARDNT LDFDDRLALT LQNSYKRVLA
     KLANPDPE
//
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