ID A0A3S9P2F2_9BACT Unreviewed; 983 AA.
AC A0A3S9P2F2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EI427_08925 {ECO:0000313|EMBL:AZQ62358.1};
OS Flammeovirga pectinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=2494373 {ECO:0000313|EMBL:AZQ62358.1, ECO:0000313|Proteomes:UP000267268};
RN [1] {ECO:0000313|EMBL:AZQ62358.1, ECO:0000313|Proteomes:UP000267268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12M1 {ECO:0000313|EMBL:AZQ62358.1,
RC ECO:0000313|Proteomes:UP000267268};
RA Bae J.-W., Jeong Y.-S., Kang W.;
RT "Flammeovirga pectinis sp. nov., isolated from the gut of the Korean
RT scallop, Patinopecten yessoensis.";
RL Submitted (DEC-2018) 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}.
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DR EMBL; CP034562; AZQ62358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9P2F2; -.
DR KEGG; fll:EI427_08925; -.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000267268; Chromosome 1.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 4.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000267268}.
FT DOMAIN 176..202
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 548..769
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 792..908
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 841
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 983 AA; 113086 MW; 4DA19C465F42EDE6 CRC64;
MLIVVVCIQF IRLKNQAQKT YVKSVRNFKM LSLLMENSHD VIFSVDTNFN YLAFNNAHVD
TMKSVYGCQI ELGKNILKYM KVNNDEDIAK EDITRAINGE VYSIIRSYGN EEKHQRAHFE
ATYTPIKSEN NIITGVSVVV RDVTDQYNSQ ENLKRSERKY KMLFHYNYLG ALIILNGRIV
DSNDTAVSLL GLELHELLGM SLDEVFINLT DNPLKEKRIV HYHNKGKKIF ILREEVIGDD
KDPQNILFIE DVTQKNKAEK ELIRVNNQAK VLLESAKSYI FSVDVNYGIV FFNTRFSSLM
ESEYGISVKV GDKINGPKYH DFFYKFRENF ERAFTNRKMF ELEFKLNQEI YLQSVFSPLL
NEKNEIYGLA IYNIDITRNK KHETQIYQLN SSLEQKVQIR TQELQQQRVK LDLALNAADV
GTWSYLLDDK FLCDSRFLEI FGLDSITYTI HDFLKFVDAS DIKKVNAVVK NISDGKVTDI
DLSFKINHPS KNVQYLQIFG RSRLNSGVYE MNGVCWNLTS QKNIEQELES AKNEAVKSSA
AKSLFLANIS HEIRSPLNAI IGLSNILYKK FEDTNQSAEF IEQLKYIYFN GEYLSELINN
ILDFSRIDAG KMSISMEKVE IINLIRMIVK VHEFSSVERG IYINLEIDKS VPEVFLTDKT
KFRQILTNLL TNAIKFTKDK TDILVKVKSV GTNFIFSVED HGIGIPKDKL KVIFDSFEQA
DKSVTRKFGG TGLGLAISKR MTEMLNGTIS VESKEGEGTL FTIVLPVKKS KIKSIDKEHT
LNLNLKFQRE DIVLVVEDNK MNQFMMKALF KQLELSIEIA ENGEDAIQKI KSKKYNLILM
DIHMPIMGGI SAAKIIRQEL KETQVPIVAL TADAYWDKRF KAFAVGMNDY LTKPINRTEL
LNILSKYLIK DKDLPKNYLD PNVHSDLIDE IRKVTVDQTM TAEAKLKRLN NISNLLQDYD
TGFVKYIDHL SEAIASEKKV DLF
//
