ID K6YSQ8_9ALTE Unreviewed; 1076 AA.
AC K6YSQ8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GARC_4270 {ECO:0000313|EMBL:GAC21212.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC21212.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC21212.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC21212.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC21212.1}.
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DR EMBL; BAEO01000062; GAC21212.1; -; Genomic_DNA.
DR AlphaFoldDB; K6YSQ8; -.
DR STRING; 493475.GARC_4270; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR Proteomes; UP000006327; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; PF00072; Response_reg; 2.
DR Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:GAC21212.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006327};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:GAC21212.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1076
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003897739"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 434..654
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 671..792
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 816..932
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 407..434
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 725
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 866
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1076 AA; 121495 MW; FBC7C46EB0DDDBA5 CRC64;
MKAAFFCSLL TCCLIATYLH AETNQSISDQ IESLRTQIQA NESSVPVRIE YLRNYFIKNP
DDYHESAFLN VWAYASLLKQ NIEVAYQRLL LARSKAETSD NNLQLAESFR IEGAVLDTIG
EYGAALEALN KAFSLYSELQ SDKVLGVYSS ISNVYNSLEN YQGTLQNSYR LLAAAQQHNN
KAYEGLAYFR IAFAQSQLEQ LQDATVNATI AEKILQQVDY PFIGVVYLLI AQINVEQGNF
EEGLKRISQS IEADRKVDYL YNEVPRLLLI ADIYQQQGNT NNAIDELKKS FENEVLRNDK
NQFLQILEKL IELTDLTGDT NSQLNFLKQY NTLYKQSFNQ KQAQMLAINN VRLNVFEKEK
EIKLLHKENE LQLQKSLIQD QNNRYQLYFT LTVFAALLLV VALLIRTRKQ RAQLNRYSQE
LKQATQAKSD FLARMSHEIR TPINAISGLT KLMQRNADNP DDMTNLRQID EASCSLLGVI
NDILDFSKIE AGKLDITTTS FQLDKTVSQA IRLQLISAHQ KNIELIQHIA RDVPLYLQGD
GLRIQQVLVN LLSNAVKFTD DGLVYVTVKN KATEQGVLLE FAVKDTGIGL TQNQMDGLFE
SFAQGDESIS RRYGGTGLGL AICKQLVELM GGKIWVESQL GSGTTFYFTL PLKEEKNQHI
SSPSKQLSNL KVLVADDINL SRQVIAEILL QANIKSDLAD GGQETLNKLR LATAKLQPYD
VLILDWKMPD IDGLQVAAII NQEFSLNKPK IIMLSAFDFS HMQQQAKQLG IKDFIEKPFS
ASELINRLQE VAFNLKTDSS PSFKEMKNVP DLSTKRILLA EDNKLNQKVA LGFLKYTKAE
VILVENGLEV IEAYKHQGNF DCILMDVQMP EMDGLTATLT LRNELKCNLP IIAMTANAMN
QDLQKSSAAG MTAHITKPIE PEYFYQVLAE ILLASPQVIT QNSQQSKLSA VDKSAINPIE
TLLIMDQAKA MQKLFVDEET FVSMLKDFVE KEPTLKTLNT LIENGAYQDI YKITHDLLPT
LTYIGADNLA KLTRSIESTI YNKTQQNNQE FAEQLTRFNQ AMLELVAKIK NQLANN
//
