ID A0A0S2HWK4_9BACT Unreviewed; 1476 AA.
AC A0A0S2HWK4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, 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 Name=luxQ_6 {ECO:0000313|EMBL:ALO14324.1};
GN ORFNames=L21SP5_00652 {ECO:0000313|EMBL:ALO14324.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO14324.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO14324.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO14324.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
RL Submitted (NOV-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};
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DR EMBL; CP013118; ALO14324.1; -; Genomic_DNA.
DR RefSeq; WP_057951879.1; NZ_CP013118.1.
DR STRING; 1307839.L21SP5_00652; -.
DR KEGG; blq:L21SP5_00652; -.
DR OrthoDB; 9796457at2; -.
DR Proteomes; UP000064893; Chromosome.
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; cd00130; PAS; 5.
DR CDD; cd00156; REC; 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; 5.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
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; 5.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 4.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 5.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ALO14324.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000064893};
KW Transferase {ECO:0000313|EMBL:ALO14324.1}.
FT DOMAIN 65..135
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 184..257
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 256..309
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 431..502
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 509..559
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 560..630
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 683..726
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1001..1222
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1245..1361
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 34..75
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1294
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1476 AA; 169917 MW; 9B087754C39B5FA4 CRC64;
MSLSNKYRKD LRKKAEAILK KQGGKNKEEL GKDLESLVEE LNIYHIELEE QNRELQLLQQ
ASEEQKNKYV DLFENAPNAY LIIDTYQHII SANKKASEML NIAQPRLKQQ KLSLFLDPEY
QDEFYFMLKN TLKQTKSISR QLAIINANEE RKTVYCTAEA FGDHRQLLRI AMVDITTQKQ
LEEENTFKAN ILENVTDCIF TINNRGNITY WSKGAKALLG FTPEKMLNTN PAKIFPNIPP
SYFSALREKS EIQLEQGFQW KAIAANKKTI WLQVKITKLN NENNTEKDTY IIVAKDITLQ
KNAEDALRSS KQQIEKILNS IDDRIYISDP ATFEILFTNI QNEQEAEHIL SQKCYKTIYE
KDQQCSYCKF NNLKKISKAD QIKKEIFVEQ TGKYYQVVEK PITWTNNKSA IMHTLTDITD
VKMSKKELLE NEEMLSNLTN AANDGIIMVD KKGTIKFWNP EASNIFGFSH DEAIGKEVHQ
LITDSKKSSS AKEALKNLAK SGNSKKFNQT FELEARKKDG SIFTAELSLA SVKLKDDLNA
IGIVRDITKR KQEEMRLQES ENRYRTIVDN VKEALYIHTT DGEFLDCNTA LLQLTQYSYN
DLQNIHPKEV IDEETGKKYF ARLQKLVEKK HLTFNTTIIK KNGEKLPVEI NANLIHYKGR
EAVLISARDI TDRIIERQKL EESEKRFRTM ADNIPDAIYI HNLEGQILDT NEKATEMLGY
KREELLKMTP LDISAIYFNF DEYEDIVKKI EEEGLVIFED KHLTKTNKKI PVQITSTVIS
YKNKPAVFSV AHDITNRKKA DKSQNKLINQ LNYLSKSATK FISFNDYEDI YRFLGKSLHL
AIENSIIVVK KYENERFQII DFYGENIDIN IQQLKAYEKG LKTFKPDPER LKKYKSGKLE
KSVDLKTLLN KKYPREFIEK INKTYQISET RVIGVTRDDV LYAGINILTE QPMDITDQEF
TQALVYQASI ALQRKNHENE LIKAKVNAEV ANNAKSAFLT NMSHEIRTPI NTILGFTEIL
SNDITDEQQI NYLKSINSSG KSLLTIINDI LDLSKIESGN MPIKHDPMSI KTLINDMEFI
FRAQAREKGL NFKISIDKSV PRLVKLDQPR LRQILQNLIS NAIKFTYQGK VELQANTANS
ENDKTDLIFK VIDTGKGISR NKLNAILEPF QQEDSSDARK FEGTGMGLSI ARKLTSLLNG
ELKIESEIDK GSVFTIHLPS IPVLETESYN VQSINTNKLK FDRERILLVE EDTNQGEIIQ
SMLEKHNLTV LTAETGDQAF AFANEFNPQL AIIDLSTQTH KSIGTAKDIR SLDQFSNLPI
IGITRHSKQE FDGMEISKYF SDIIKPPLTK SAIFKQIMKY IECKKTLSKD DNTNTETFDF
SSYETTSLEN ALNSLKENAS PIWDLLEKRQ PLNKVKSFNH VIYKTGEQEH ILILKQYSKQ
LTESLKAFDI IQMRKLLKEY PGIIKAIEKQ IDKNKK
//
