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Database: UniProt
Entry: A0A0F4PNQ9_9GAMM
LinkDB: A0A0F4PNQ9_9GAMM
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ID   A0A0F4PNQ9_9GAMM        Unreviewed;       928 AA.
AC   A0A0F4PNQ9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CWC05_18100 {ECO:0000313|EMBL:TMP85546.1}, TW72_05635
GN   {ECO:0000313|EMBL:KJZ00994.1};
OS   Pseudoalteromonas ruthenica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=151081 {ECO:0000313|EMBL:KJZ00994.1, ECO:0000313|Proteomes:UP000033664};
RN   [1] {ECO:0000313|EMBL:KJZ00994.1, ECO:0000313|Proteomes:UP000033664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3137 {ECO:0000313|EMBL:KJZ00994.1,
RC   ECO:0000313|Proteomes:UP000033664};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
RN   [2] {ECO:0000313|EMBL:TMP85546.1, ECO:0000313|Proteomes:UP000305874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2897 {ECO:0000313|EMBL:TMP85546.1,
RC   ECO:0000313|Proteomes:UP000305874};
RA   Paulsen S., Gram L.K.;
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000305874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2897 {ECO:0000313|Proteomes:UP000305874};
RA   Sonnenschein E.C., Bech P.K.;
RT   "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT   Pseudoalteromonas.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:TMP85546.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S2897 {ECO:0000313|EMBL:TMP85546.1};
RA   Sonnenschein E.C., Bech P.K.;
RT   "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT   Pseudoalteromonas.";
RL   Submitted (SEP-2019) 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   -!- 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:KJZ00994.1}.
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DR   EMBL; JXXZ01000005; KJZ00994.1; -; Genomic_DNA.
DR   EMBL; PNCG01000024; TMP85546.1; -; Genomic_DNA.
DR   RefSeq; WP_045979501.1; NZ_PNCG01000024.1.
DR   AlphaFoldDB; A0A0F4PNQ9; -.
DR   STRING; 151081.TW72_05635; -.
DR   GeneID; 58227971; -.
DR   PATRIC; fig|151081.8.peg.2067; -.
DR   eggNOG; COG2205; Bacteria.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000033664; Unassembled WGS sequence.
DR   Proteomes; UP000305874; 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; 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; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF14938; SNAP; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
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; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS50005; TPR; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000033664};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..928
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033221770"
FT   TRANSMEM        418..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          140..173
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          220..253
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          480..697
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          719..833
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          843..928
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   COILED          446..480
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         768
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         882
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   928 AA;  104346 MW;  323B77BC7E9D2C2A CRC64;
     MSQRKLPRLL VCIQLLVCSL FTSLSYGDAL IDDIRSQPQQ LQRDYAISKL AQPLSEPQQL
     AVNAFIAKQF FEDSNYEKAA RYYLRAEQLA AKHGTVIEHS RYAQMQGVSH YYRGQDLTAI
     EDYLRAIEII EQIDKPIIAA HLYNNIGLAY SGADQIEAAI ASYSKAKELY DEYGDEYDQV
     NIMHNIAVAY MDWYRFEAAF DIYEQIGDSF ERLGDTIGQA QMETNLGSIY QSRMDFEQAE
     IYYQKALVKY QENGDRPNHI VNLIRLAELN FVQGRFDAAY TQMRDAQAQA EVMDNLHYNS
     NIKEIEAKLL FAKGQYKQAQ QALREVYTMR EQVTDDKASP AISLIELLVT AAQGDHVKSA
     LLYERYERQQ QEMLSNKIAS SLNDFQAKYN ATELQQQVDS LKQQQQLDKL EAQQRRQMTF
     LAAGILILAF ISIVLLFRRS AERKATAMLE DKVKQRTKEL EELADQLSAA NEIKSQFLAN
     ISHEIRTPLT SIMGQAQAII EGDVPAEQVA KELRVIYNNS QHLGELINDV LDLSKIEANK
     LELVISTVSI CSLLADINAM FQPSASQKGI LFRINNKLPA SFGAEFDYIR VKQVLVNLCS
     NAVKFTEQGE VELAITADEQ GVCFRVKDTG IGIAEDKLDA IFANFSQGDN SISRRFGGTG
     LGLSLSQQLA QIMGGDISVS SVLGQGSTFS FYIPCRCMEM DERSNDTIQA ARALSFSGEV
     VLAEDHEDNR RLIERLLTNL GIKVHSAANG EQAVELTLQH CPDLVLMDIQ MPKMDGLEAL
     NLLRQCGYTQ PIIALTANAM THDIERYKAA GFTNHLAKPI EKEEFCRTLE HFLNVEIDAR
     AAQSVDMSDL HESFMHTLPR EIESLVNAHA RNDLDEIKAV AHRLAGAAQM FASQTIAELV
     CDIELAAKYQ DKEQVGVLIE DLANLELE
//
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