ID V5BRI6_9GAMM Unreviewed; 1211 AA.
AC V5BRI6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=frzE {ECO:0000313|EMBL:ESS67173.1};
GN ORFNames=MGMO_171c00150 {ECO:0000313|EMBL:ESS67173.1};
OS Methyloglobulus morosus KoM1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methyloglobulus.
OX NCBI_TaxID=1116472 {ECO:0000313|EMBL:ESS67173.1, ECO:0000313|Proteomes:UP000017842};
RN [1] {ECO:0000313|EMBL:ESS67173.1, ECO:0000313|Proteomes:UP000017842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KoM1 {ECO:0000313|EMBL:ESS67173.1,
RC ECO:0000313|Proteomes:UP000017842};
RX PubMed=24356841;
RA Poehlein A., Deutzmann J.S., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of the Methanotrophic Gammaproteobacterium
RT Methyloglobulus morosus DSM 22980 Strain KoM1.";
RL Genome Announc. 1:e01078-13(2013).
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 -!- 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:ESS67173.1}.
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DR EMBL; AYLO01000156; ESS67173.1; -; Genomic_DNA.
DR RefSeq; WP_023496442.1; NZ_AYLO01000156.1.
DR AlphaFoldDB; V5BRI6; -.
DR STRING; 1116472.MGMO_171c00150; -.
DR PATRIC; fig|1116472.3.peg.3836; -.
DR eggNOG; COG0643; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000017842; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProt.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; 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; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000017842};
KW Transferase {ECO:0000313|EMBL:ESS67173.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 436..539
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 707..921
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 923..1058
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1079..1195
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 568..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 482
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1128
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1211 AA; 133175 MW; 0C140B048751BC5B CRC64;
MKKPDLNELG NLAAYFERLA DQAAQRGCYG LQDANLVLAE AVRVLQSDNP ASNNLFPLVG
EWFDLVEKFT QAPKQTASEM TTYLRRPELN IPMEDEEFAM LGEQLLNDAN AAALSPNEAS
DITVARTTPS IAEQHITDEQ VAYIEQLANQ AAAEGLYGLQ DVNLLLAETL RELSGDAIVD
SGLISALSGW HDLLVDYRKE PRVKAEALIN FLRHPGLKIP MGDDEFAMLQ EQLTTEAEAN
VTAQEQVVDI QAVESIPEGD PSSDKNSLSG VSRIAQELVD LLLMQIGQIR DYLQSITIGN
NESLLDSLQE VGDDLERFSN MAKTAGFGGL SQVATHVTGN VQSFQASIEG FTTERLDLLL
DWTGQVQEYL PSFNDSDAGQ LILVGLTDEQ WPMPLPFEEM VAILQQIRAE SSVVGEDPVL
TRMEKATDED ISLVLPGDVN QELLEILLQE LPIQTQQFSE AVQRLHAGGS EQDVQLAQRV
AHTLKGSANT VGIKGIAVLT HQLEDILLAC ANEQKLPNRA LANSLINAAD CLESMSESLL
GVSPPPSDAK VILQEILDWA NLIDKVGLPE RDDETTSPVA QERGVTESEE TDSPSQLQAT
MIRVTSEQIE ELFRFSGESI ILNSQASDSM RRMKKQMHAM KVQFSLLQEL GAELEQLIDL
KDLTGRSFGV VDTNFDVLEM DQYNELHTAS RRMAEAAIDA RELSLDVTKE LDRVSEILES
QQRMVVDTQE VVMQTRLVAI STIAPRLQRS IRQTCRMTGK QSELTVKGDT IMIDGDVLNA
LVDPMMHILR NAVDHGIESP DERRAHGKPP VGQIAFEFDR EGNNILVRCR DDGKGLDYEA
IRAAAESRGL LQSGQDVTDE ELKSLIMRPN FSSRTVSTQT SGRGVGMDVV RAQILNMGGT
LNLHSVQGQG MTIELRVPLP LSMTYALLTY VGHYRVAVAN KGINQIVYSK EGEVILEGNK
ETLLLEGVIY PVARLIDLLH IADHRKIPRP YDAILLVQNE NQTTAVLLDA IFDSLEVVIK
GLGRYLGKVP GYIGATILGD GTVTPVVDIP ELLRAPVRVL TGDYVAPVEM ADPTLNLPTV
LVVDDSLSQR RALEQLLADA GYRVRSARDG IEATDILAHF KPDVVLTDLE MPRMNGIELT
AHIRSHANTS SLPVIMVTSR TTQKHKKMAE DAGVNAYITK PVREEDLLTE MENLMAQQTG
NVQAQNIAQL S
//
