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Database: UniProt
Entry: A0A0C5VSU1_9GAMM
LinkDB: A0A0C5VSU1_9GAMM
Original site: A0A0C5VSU1_9GAMM 
ID   A0A0C5VSU1_9GAMM        Unreviewed;       985 AA.
AC   A0A0C5VSU1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=YC6258_05211 {ECO:0000313|EMBL:AJQ97241.1};
OS   Gynuella sunshinyii YC6258.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Gynuella.
OX   NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ97241.1, ECO:0000313|Proteomes:UP000032266};
RN   [1] {ECO:0000313|EMBL:AJQ97241.1, ECO:0000313|Proteomes:UP000032266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6258 {ECO:0000313|EMBL:AJQ97241.1,
RC   ECO:0000313|Proteomes:UP000032266};
RA   Khan H., Chung E.J., Chung Y.R.;
RT   "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT   YC6258T gen. nov., sp. nov.";
RL   Submitted (JAN-2014) 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; CP007142; AJQ97241.1; -; Genomic_DNA.
DR   RefSeq; WP_044619030.1; NZ_CP007142.1.
DR   AlphaFoldDB; A0A0C5VSU1; -.
DR   STRING; 1445510.YC6258_05211; -.
DR   KEGG; gsn:YC6258_05211; -.
DR   PATRIC; fig|1445510.3.peg.5174; -.
DR   HOGENOM; CLU_000445_22_1_6; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000032266; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd10322; SLC5sbd; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032266};
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..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        399..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        427..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        468..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          626..670
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          759..976
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   985 AA;  110154 MW;  59A677D0000B8EE2 CRC64;
     MTFSLSLLFA IGFGYLLLLF LLAHVVEKEW IAREWARHPL VYVLSIGVYC SAWAYFGTTG
     LAYEYGYGYL TYYMGLSAAF LLYPFLLKPF LKITKNHSLG SLADVFAFRY HSRWAGTATT
     ICMLLAILPL LALQIQAITD ATVILAPDTN ATPVGLAFCA MMIAFTTLYG ARQIHPRERH
     RSLIFAIAFE SFFKLLMFVG LGIVAVFYVF ETPEKLQQWL NGPGFILRNR LNTMPIQTWM
     LMSLLFIFAP LTMPHLFQAL LRENRNPTHL RYATWAVPIY LFLMALPVLP IMWAGMYLGQ
     PTNPEFYSLA LGLGLQSPVI TILAYLGGVS AASGLLIVAT LAMASMTLNH VILPIHTPKG
     DEDIYHWLLW TRRGLIVTII LAAYLVYMLL GQIHNLSSLG IASFVGVLQF VPGIIGTVFW
     SRANRKGFLT GLVAGMLIWF ISIFYPLLVD SFSLTYRLPL RFALSESAWA YATSISISVN
     LVLFLVVSWF TETSEEEKKA ARACSQDALA DTKRRQLVAR SSDQITEALS TALGKVSAER
     EVNRVLKELN LPVGEYRPFA LRRMRDRIET NLSGLMGPSV AQTIVQRYLP YASDDEFGKE
     DINLIESQLE GYHTQLTGLA AELDNLRRYH RQTLENLPVG VCSIGSDTEV LMWNPIMTEI
     TGIEAKDIVG SHLNSLPLQW QTLLSRFMQG LSTHAYKKEL VIGSRKRWYN LHKASLPQGE
     KTLSEGTVIL VEDQTEIQML EDELVHTERL ASIGSLAAGV AHEIGNPVTG IDCLAQDLLY
     ESDSPMVKEA AEQIREQTRR VTQIVQSLVN YAHAGSTTGK SEHIAHPLHM IVHEAIKLLE
     LSKKSRDVEF INNVPQQVEV ICDPHRLSQV FINLLNNARD ASEPGSYVAV NLHEPENNHF
     VTVEVLDRGS GINPEHLDHI FEPFFTTKDV GKGTGLGLWI AYSIVEEHYG QIQVESPAFK
     VEGIGTSVII TLPKANRPSN PEEQL
//
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