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Database: UniProt
Entry: A0A1I6GRB0_9GAMM
LinkDB: A0A1I6GRB0_9GAMM
Original site: A0A1I6GRB0_9GAMM 
ID   A0A1I6GRB0_9GAMM        Unreviewed;      1148 AA.
AC   A0A1I6GRB0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04488070_1100 {ECO:0000313|EMBL:SFR44587.1};
OS   Pseudidiomarina maritima.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Pseudidiomarina.
OX   NCBI_TaxID=519453 {ECO:0000313|EMBL:SFR44587.1, ECO:0000313|Proteomes:UP000199424};
RN   [1] {ECO:0000313|Proteomes:UP000199424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7285 {ECO:0000313|Proteomes:UP000199424};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC       family. {ECO:0000256|ARBA:ARBA00006434}.
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DR   EMBL; FOYU01000001; SFR44587.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6GRB0; -.
DR   Proteomes; UP000199424; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd10322; SLC5sbd; 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; 1.
DR   Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 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; IPR038377; Na/Glc_symporter_sf.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   InterPro; IPR000014; PAS.
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; 1.
DR   PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
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); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
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};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        403..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        434..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        468..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          797..1008
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1029..1146
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          728..790
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1079
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1148 AA;  127725 MW;  6E5F1F0C191CB2EB CRC64;
     MTLLLILASL AYIALLFAVA HWGDKPNSLA NKISYKPIIY SMSLAIYCTS WTYYGAVGNA
     ATDGWAYIPI LLGPFLLFIF ALPLLEKLVS VSKQQNITSI ADFIASRYGK RQRLALFVTL
     IAALATIPYI ALQLKAVGLT FVVLTENTSA LTQFSINELV AAGIMAVFAM LFGTRHIEVT
     EYRNGMILAI AFESAVKLLA LLAAAVFAYF LFNDVSPVSM WEQVTTPSSK AWSWEALTEF
     DFIVQTFMAA GVILCLPRQF HVAVVDNVNV NHLKTARWGF PLYLVLVAVA IVPIALSGGL
     FFGNGIDGDT YALRLPLLHD QTWLAVFIFI GGFSAATAMV IIASVTLSTM VTNDVIMPVI
     LQRRSRFPTS FQKRLLFIRR VAIAIILLLS YLCYYFWAAG TGLVSIGLLA FSVVLQLLPA
     VLGGLYWRRG HARGVYVGLG TGLIAWLFAV AVPMYLPHDS TDTSIITQGT VISLAVNTAF
     YFVFSLLAQP RLIDRIQATA FVKPRTRVQE HTVGRHHQAT NGDMMLLLQT FVGEQRTAQL
     LDYFAEAQGN DSSHTNKEDV ASREFIDYVE RVLTGVLGAA TARSLVEAAL RDRRLHLEEV
     VHFFDDTTQA LQTQQAILFS SLENLAQGIS VVDADLRLVA WNKRYLDLFD YPDGMVKPGQ
     PIATLIRYNA ERGECGPGEI DELVAKRLKH MQVGSPHRFI RRRGDGRVIE MVGNPLPNGG
     FVTSFTDITE HVETQQALEE ANIDLEQRIN VRQKKIREIN NELTEEIERR RKVEVELKKA
     TQQAEEANAS KTRFLALASH DILQPLNAAR LYLSAMDENN LNHNNLQLVS KLDTALASTE
     HLLSTLLQIA KMDQGALQPS FRHVRLSTIL EPLIHEYGVL AEQRGITLKT HLHDGVVYTD
     PTYLRRIIQN FLSNAVKYNR DQGKVLLAVR KRGEHLLIAV YDTGPGITAQ QRHRIFDAFY
     RGSQTRVEGV GLGLSVAKRM SEQLHCELRL KTVEGSGSCF SVQVPLGNPS QVYEKPQQAN
     TADVNRGMQV VCVDDDQENL SALRALLEKW GCTVETFTSS ATALEYASTH ERPDGILLDY
     QLGDDEHDGL SLARALRHYW GDTLSGALVT AMRDDSVRKQ AREQNLHFLA KPVKPAALKS
     LLKYLERQ
//
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