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Database: UniProt
Entry: A0A094JH30_9GAMM
LinkDB: A0A094JH30_9GAMM
Original site: A0A094JH30_9GAMM 
ID   A0A094JH30_9GAMM        Unreviewed;      1143 AA.
AC   A0A094JH30;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HR45_03610 {ECO:0000313|EMBL:KFZ38527.1};
OS   Shewanella mangrovi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=1515746 {ECO:0000313|EMBL:KFZ38527.1, ECO:0000313|Proteomes:UP000029264};
RN   [1] {ECO:0000313|EMBL:KFZ38527.1, ECO:0000313|Proteomes:UP000029264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YQH10 {ECO:0000313|EMBL:KFZ38527.1,
RC   ECO:0000313|Proteomes:UP000029264};
RA   Liu Y., Zeng R.;
RT   "Shewanella sp. YQH10.";
RL   Submitted (JUN-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}.
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:KFZ38527.1}.
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DR   EMBL; JPEO01000002; KFZ38527.1; -; Genomic_DNA.
DR   RefSeq; WP_037439775.1; NZ_JPEO01000002.1.
DR   AlphaFoldDB; A0A094JH30; -.
DR   STRING; 1515746.HR45_03610; -.
DR   eggNOG; COG0591; Bacteria.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000029264; 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; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 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; NF041832; near_NosP_CTERM; 1.
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   Kinase {ECO:0000313|EMBL:KFZ38527.1};
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:UP000029264};
KW   Transferase {ECO:0000313|EMBL:KFZ38527.1};
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..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        406..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        434..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          787..1001
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1022..1139
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1073
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1143 AA;  125690 MW;  CAFE0BA221FCC738 CRC64;
     MNLTWLVAAF ALCYVCLLCL LAWGAERWFS NSTKKLQHWI YALSLAVYCS SWSFLGTVGQ
     SVNDFWSFVP IFIGPILVFL LGFGLLRKMV IVSKAQNITS VADFIAARYG KSQPLAVFIT
     LIAMFGIMPY IALQLKSMVF AFNLFQPKGE PLNGTLVALL ISIWLAVFAI LFGTRKLDAT
     EHNPGMMLAI AFESLVKLTA FLVLGIVVVF GVFGGFGPLW EQASSAGIIQ EPNMRLESIV
     PDVLVGMAAF LCMPRIFHVM VVEAQNERNL RKARWVFPLY LVLFASFVGP LALAGKLLLG
     DTVTPDTYVI NLPLAMGKEW LAVIALLGTL SAATGMVIVA VVTISIMISN EWLVPVLLRT
     GQIKRGNFGQ FSTQLLYVRR ISIVLILAMG YVAYLSFQHN DSLSHLGMLA FGSFAQLAPA
     LVGGLYWKRG NRSGVMLGLA VGFVLWGVLL FRDAAISGDL FTQGMSTFTD VTPNIHDILT
     SLVANFIFYI LGSVWFRAGV VERIQASAFV IPGQMRNSGN RRAVQISQQD LLILASRFVS
     PTRAYESFSR FSPEAVRSDS WHKSASRGLI NHTEHLLAGV LGASSAAVVM DSVLEGRDLA
     LDEVFSLVDD ASSQVLLSQD MLRAAIEHAN EGMSVVDKDL NLVAWNYRYE ELYRYPKDFL
     QPGMPIAKVI RFNAARGYCG VGSIDEHVEK RLNHMRAGSA HSSERQRKDG KVIKIQGNPM
     PDGGFVMTFT DITQYREQQK ALQASNENLE ARVRERTYEL ALLNSQLLEA KAQEEMANAS
     KSRFLAAVGH DLMQPLNAAR LFTASLTQHP DVALDVQQTL SHINGSLKNA GELLTDLLDI
     SRLDSGKVDV KRRDFSIEEI LSTMAVEFEA MSGDSKIRFE VVSSKVTVNS DPALLRRIIQ
     NFLTNAFRYA KGGKVLLGCR HRKGMLEIQV LDTGCGIEPE QLKAIFQEFK RIDNPHSKSA
     NGLGLGLAIA ERISKVLEHE IKVYSIHGKG SMFSVAVPIG SKATEPKLKN MTAAVKTLAG
     VKVLCIDNEE AILAGLESLL TRWQCDVICA NDIDDARIKL GLKGVAPDIV LADYHLDDGK
     NGVDAMDAIR AAYGDTLPGI LITANTNKAV IDDVEQRGYH YMAKMVKPAA LRALISSLVR
     QRR
//
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