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Database: UniProt
Entry: D8F2Z3_9DELT
LinkDB: D8F2Z3_9DELT
Original site: D8F2Z3_9DELT 
ID   D8F2Z3_9DELT            Unreviewed;       762 AA.
AC   D8F2Z3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NPH_2132 {ECO:0000313|EMBL:EFK09859.1};
OS   delta proteobacterium NaphS2.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK09859.1, ECO:0000313|Proteomes:UP000003834};
RN   [1] {ECO:0000313|EMBL:EFK09859.1, ECO:0000313|Proteomes:UP000003834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NaphS2 {ECO:0000313|EMBL:EFK09859.1,
RC   ECO:0000313|Proteomes:UP000003834};
RX   PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA   Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA   Lipton M.S., Deboy R., Methe B.A.;
RT   "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT   Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL   PLoS ONE 5:E14072-E14072(2010).
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:EFK09859.1}.
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DR   EMBL; ADZZ01000261; EFK09859.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8F2Z3; -.
DR   OrthoDB; 9805967at2; -.
DR   Proteomes; UP000003834; 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; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.290; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; 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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003834};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          223..275
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          349..401
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          402..475
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          534..759
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   762 AA;  86192 MW;  A021C6D71A6CFB33 CRC64;
     MEKRRRFQNV HLSLSFRLIF WVGLILAASI AAWAYYNIGH QKERAVENIV KVADRLGNTI
     RLGVHYAMML NSRDDITQII KNMGKQEGIK SIRIYNKAGQ TSYSSNAKKA EPMMNMKEGA
     CLICHNTDPP LVKVSLAGRT RIFEGPRGER FLGIISPIYN QPGCASAACH FHPEKTKVLG
     ALDVVVSLKD TYREIFAYER GIILMAAFIF LLTSGFMIFF LLRFVNRPIG KLIEGTRHIG
     RGEYDYKVDL KRKDDMGQLA DAISHMGKKI GEKQDELNKQ KTEYWELFES APCYITVQDR
     NFRLLKYNRE FAEQFDARSG DYCYQVYKGR SERCEICPVQ DTFDDGQPHH SEEEGINRDG
     TKSCWMVRTS PVKNNAGEVI AAVEMSLDVT AMKHLESEVK KSEEKYRIIF STIPNPVFVL
     DQTKLNILDC NDNVTSVYGY PKEEVLNTSF LDFFGPRERR QYESRMKAST VIDSAKHYAK
     DGSAIYVNIR VSSTEFSGEA VFLVTISDIT ERLLAEQQLI QASKMATLGE MSTGVAHELN
     QPLSVIKTAG SFLHKKALKG GKIDDDTLKT LTAEINSQVD RASKIINHMR EFGRKSDVVK
     EEVQLNDALT RALEIFRQQL KLREIKVALD LQQHLPTVMA DSNRLEQVFI NLLINARDAI
     EAKWWGNVDP KDKAKKITLR TRKKNSFAIV EIADTGIGIS KAVIDKIFEP FFTTKQVGKG
     TGLGLSISYG IVRDYDGTIS VESEEDKGST FTIRFPVSGS DR
//
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