ID A0A150AQR2_9BACT Unreviewed; 770 AA.
AC A0A150AQR2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AVL50_02625 {ECO:0000313|EMBL:KXX72131.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX72131.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX72131.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX72131.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:KXX72131.1}.
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DR EMBL; LQAQ01000016; KXX72131.1; -; Genomic_DNA.
DR RefSeq; WP_062615098.1; NZ_LQAQ01000016.1.
DR AlphaFoldDB; A0A150AQR2; -.
DR STRING; 1775430.AVL50_02625; -.
DR OrthoDB; 9806995at2; -.
DR Proteomes; UP000075267; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR004010; Double_Cache_2.
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; IPR033480; sCache_2.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF08269; dCache_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01049; Cache_2; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000075267};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 503..762
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 457..494
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 770 AA; 88989 MW; 7394D11C0C639CE9 CRC64;
MKLFEQNTTH KEKKERVSEA TFIPVMTLSV IAITFLVGIW SIKELRDYKL DVSQLEIEFT
NKQKNVTVNE VNNAFKYIQY LEKNTEKRLK ENLVNRVDEA FQIVDNIYKR NNGKLTQKQL
IELIKDSLRP IRFNSNRGYY FIDHVDGYAV MNASSPESEG LPIMDLQDAR GDYFIRKEME
IAKTKGKGFF QYYWIKPGQD GDKQYPKTSY LRYFEPLGLV IGTGEYMDNV TRDMQKQALE
RMSSIQFGKD GYLFVNKRGN PLLMNWEYFD EAYQLTEEQH LSLPITDENG DTTYFKDLPF
FLMNTEKKGG FYYYDYKKPN SDEIKRKFSY IIYFKEWDWT IGAGVYLDEL DDQIATKRSL
LITELTTELF RILSLSTLLI AILWWRLRKV ATGITNNIEE FSNFFDEASK EHVKINKDRL
AYAEFDQLAT LANKMLDDRE NDRRKIIEAY HEIQTSEEEL RQQSESLLYT NQKLEEAMQE
LKSAQVQLIN SEKMASLGQL TAGIAHEINN PINFVSSNVQ PLKDDIDDLI RLLESCNDLT
KEFESKEAFQ QRVSEINELA EEIEISVITE EIKELINGIE EGALRTKEIV LGLRTFSRLD
EDTFKSANIN EGIQSTITIL NNKARKKDIS VEVDLQKDLP EIKCLPGRLN QVFMNVINNA
IQAVDENTGK IKISSSFTEG DEHINIKVRD NGEGMPQAII DKIFDPFFTT KEVGEGTGLG
LSISYGIIKK HGGEIMVSSK YKNDSSGEES FTEFSIILPL IGEDDLKNEY
//
