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Database: UniProt
Entry: A0A1G6CUK8_9GAMM
LinkDB: A0A1G6CUK8_9GAMM
Original site: A0A1G6CUK8_9GAMM 
ID   A0A1G6CUK8_9GAMM        Unreviewed;      1125 AA.
AC   A0A1G6CUK8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN02927930_01385 {ECO:0000313|EMBL:SDB36563.1};
OS   Pseudidiomarina indica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Pseudidiomarina.
OX   NCBI_TaxID=1159017 {ECO:0000313|EMBL:SDB36563.1, ECO:0000313|Proteomes:UP000199626};
RN   [1] {ECO:0000313|Proteomes:UP000199626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10824 {ECO:0000313|Proteomes:UP000199626};
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; FMXN01000007; SDB36563.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6CUK8; -.
DR   STRING; 1159017.SAMN02927930_01385; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000199626; 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   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   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   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   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:UP000199626};
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        60..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        194..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..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        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        436..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          775..985
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1009..1123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1056
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1125 AA;  124585 MW;  D1EA4B7808EF3331 CRC64;
     MLSTGLTILL AMAYIAVLYS IAYRGERRSS NQHKPYRYAL AQGIHCTTWA FYGTMTQSAF
     YGWSVAPTYI GAMLVFLFAH RLQMRLLHVC KQQNLTSISD VISQRYGKSP TLAIAVAIIA
     LIGIIPYIAL QLRAVSSSFG AVTGLTATPL PWFIDVVVLV AIAMIGFAIL FGTRRMSLAE
     QHAGLMDAVA FESVVKLAAF MGVGFYVSYV LFDNVTDIFV QASQQPAITA VLAGQPHGGF
     VYMTHIILGA ISMFCLPRQF HVSYIENNDP EELKTARWAF PLYLFAINLF ILPLALAGLL
     LVPEAMHSDT LMISLLLTAD DPGITAIAFI GGLASATSMV IIATLALSIM ISNDVVMPLW
     LKSTKRKFRN EIFTPQKILS IRRTTIALII VFALGFHKLT EANLPLVNAG LLSLALLAQL
     APALLGGIIW SRGNRVGASV GITMGTLLWF GLLFLPSLQR DPGLSDIALS SGVLVSLSVN
     VLCYFLFSII TKASPIETQL RALYTDPQGD HTEFYPHHAI SWGRLRQLLT RFFNYAELER
     LSERLNHNLA VAPADELVPG AILVKIEREL SAVIGTAASR ILLDTVTQQP AVPIAHVVTW
     ATEASQLYKF NRELLQASVE NIPQGISVID QELRLVAWNQ RYVELFSYPP NFLQAGMPVA
     ELLRFNAQRG LIATAAASDI DEEVEKRLNY LRHGSAYRYQ RQQGEFVIEL QGNPMPGGGF
     VTTYTDITEL VAAQRALEQV NIELEQRVAD RTAQLLAAKQ AEERAHQSKS KFFAAVSHDL
     MQPFNAATLF CDLLAQRADP SSQQLVRQVQ QSLKNAEELL TMLLEMTRLE AGNLPVNKQH
     TALHDVIGPL VENQRIIAAD KGVEVHYVPT RATVYTDRKM LSRVVQNLLS NAIRYTDHGK
     VLIGTKRCGT QLQIRVYDTG RGIPADQRNK IFTEFHQVHQ QGGNPGLGLG LAIVDRMCRL
     LELPLTLTSQ VGQGTLFAIT LPEVHWPPQT TSSPELQTSH DEEFLHGQVV WILDNDPQVL
     QAMEQLLIAW GARVHTALNR EQLPWHQPPP QLLIFDYHLD EQDTGVAVLT KVREHYQLPE
     LPAIINSADP DETVREEVIA TAALFTPKPI KTAALKRLIK RLVND
//
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