ID A0A2N1DCZ8_9ALTE Unreviewed; 1642 AA.
AC A0A2N1DCZ8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CXF95_09015 {ECO:0000313|EMBL:PKG99378.1};
OS Paraglaciecola sp. MB-3u-78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=2058332 {ECO:0000313|EMBL:PKG99378.1, ECO:0000313|Proteomes:UP000233828};
RN [1] {ECO:0000313|EMBL:PKG99378.1, ECO:0000313|Proteomes:UP000233828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB-3u-78 {ECO:0000313|EMBL:PKG99378.1,
RC ECO:0000313|Proteomes:UP000233828};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) 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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:PKG99378.1}.
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DR EMBL; PJCF01000004; PKG99378.1; -; Genomic_DNA.
DR Proteomes; UP000233828; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00062; PBPb; 1.
DR SMART; SM00448; REC; 2.
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; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000233828};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 748..801
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 895..1116
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1133..1253
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1282..1398
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1442..1535
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 724..751
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1184
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1331
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1481
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1642 AA; 181423 MW; F6B97FE86BDB6F50 CRC64;
MVTGFYYKKE DFLVGTMIDS LSKFIDKGLK RQIFCLTGFL NSLRCCSLLL LLTAIAPIVN
AQSLDLNFSN EELAWIADNP VIRVHNETNW PPYNFNVDGE PTGFSIDYMR LLAKQAGLQV
EFVSGPDWNE FLDMMRSGDL DVMLNIVDTP ERREFLLFTS PYSITSPVLA IQEHVTGIAS
LNDLVGRTVC IPQGSSTEEF LRQNYSDLNL LPLNDATACL HAVADGRAFA SVGGFSILDY
LIKSTKVPGV KIANIEVDPN MASVMSIATS IGQPLLRNIL QKALDSLDRT AVTDLRQQWL
GSPPAITGVG NLSILWWLVG GVFGLFLLLM LLNVISKRFS SDSGVVLQTG TLRFRIIIYS
SLSIFVITIS IIGWFALAQI KGKILMDMKN NLENVLITTN QRLEMWVDSR VSLLTQVARN
TELIAAIDGL LRIKVNPDAL TQSEELATTR LVLAQYREEL ELGFFIINRE GISVGSARDN
NIGIQNLIAD QRPKLLERVF AGEAVFVPSI YSDVVIGDKD IAHSISIFIA VPIKRKDGKV
IAALTMRLDP AQGFTRVMQL SRVGESGESY AFDQNGTLLS GSRFEDDLRQ IGLLGEGESS
IMNIQIRDPG VNLTQGFRSD VPRKQQAMTL MADSAIASKV NSRNQQSPVQ SNLIGYGDYR
GVPVFGAWLW NGNLGIGLTS EIDVDEALST YLTVQQTAFG VLGITLFLAL GGIVLILVTG
ERTNKILLRA RDELEDRVEE RTQELKKATK KSELILENAT DGILTIDDQQ RVVGFNPACE
QMWGYGADEV LGHEITMLIP EYARKDHLAN VHRFRDRTTA GISLESRGLK LFGLTKSGVV
FPTEVGITKN LIDGEILYSA FIKDITDRVK ADTEILEAKN AADAANQAKS DFLANMSHEI
RTPMNAIIGL SDLALRTSLT PKQQDYLNKV HSSANSLLGI INDILDFSKI EAGKLDMEVI
PFSLDEVLES LATMISVKTQ EKDLELLFSR ASDVPVNLLG DPLRLGQILI NLSNNAVKFT
ERGEILLRIS LVNQKADRAT IKFSVEDTGI GMSQEQMGKL FQSFSQADTS TSRKYGGTGL
GLTISKQLVE MMGGKIWIES EPGKGSKFIF DIHLDINPNP QDKKLSSDLD GLKVLVVDDN
PHAREILEQY INDFGLEVEC VAAAEEAFEK LIGVDQPFDL VLMDFIMPNG MDGVTATKQI
KQKLKLKKIP KVILVTAYGY GDYADMDGVS LLDNELNKPV NPSLLLDTIM ETFGHQILGN
AKGSRQSLGI DKEALDKIRG AKILLVEDNA INQQVATELL EAELLVVDVA NNGKEAVEDF
ELNNYDCVLM DVQMPIMDGY TATKLIRQKQ QYADLPILAM TANATQEDKE SALAAGMNDH
ISKPINPTVL FNTLVKWIKP GDREIPETIK IDENNTPEAN TDGIEQIRGL SIEEGLKHVN
GNKKLLNKLI MDFYNDYQNV LLTIEQALSL ENFDEVQRIA HTLKGIAGTI GALSVQEQAG
NLELAIKNNQ KELFESTLEE LVVVLQPLFE QLKLVASSNS QQADDSEVYI LESVETVSEK
ITALAQLLEE MDPDSEEQTE DLISSLKGYN QKVLLSKLKK QVAGFEYEEA QKILDLVKQN
IIDKSEAGLR LMDNSDDVID PI
//
