ID A0A143HJL6_9GAMM Unreviewed; 1167 AA.
AC A0A143HJL6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A3224_04335 {ECO:0000313|EMBL:AMX01915.1}, SAMN05660479_00066
GN {ECO:0000313|EMBL:SFB67056.1};
OS Microbulbifer thermotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX01915.1, ECO:0000313|Proteomes:UP000076077};
RN [1] {ECO:0000313|EMBL:AMX01915.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|EMBL:AMX01915.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA Lee Y.-S., Choi Y.-L.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFB67056.1, ECO:0000313|Proteomes:UP000181967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19189 {ECO:0000313|EMBL:SFB67056.1,
RC ECO:0000313|Proteomes:UP000181967};
RA de Groot N.N.;
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; CP014864; AMX01915.1; -; Genomic_DNA.
DR EMBL; FOKT01000001; SFB67056.1; -; Genomic_DNA.
DR RefSeq; WP_067151976.1; NZ_JAPHQH010000002.1.
DR AlphaFoldDB; A0A143HJL6; -.
DR STRING; 252514.A3224_04335; -.
DR GeneID; 76607281; -.
DR KEGG; mthd:A3224_04335; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000076077; Chromosome.
DR Proteomes; UP000181967; 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 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; PS50112; PAS; 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}; Reference proteome {ECO:0000313|Proteomes:UP000076077};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 627..666
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 804..1020
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1042..1158
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 742..797
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1092
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1167 AA; 128338 MW; 9B29B44C38FEB08A CRC64;
MIGKPFLLVF ALLYVALLFL VAWRAERRKQ WLPRYRPVIY ALTLAVYCSS WTFFGAVGQA
VNSTWSYLPI YLGPMLLFLF GGAFLRKLML VSERQKVTSI ADFIGSRYGK SQGLSALVTL
LAIVGSLPYI ALQLRALTMA WDAIGEGPAA GAPGGLDSAF ATALMMGVFA MLFGTRHLEG
RERNRGVVAA IALESVVKLF SFSAVAGLAL WLLLGHERYT AVDLRLDPLV PDANFLIQTF
LATTAIICLP RQFHMAVVEF QDSRDLRTAR WLLPLYLGLF SLLILPIALA GRPLLAEGLL
EPDSLVLTLP FTSGSNALTL LAYIGGFSAA TGMVIVAAVT LAVMISNELV APLWLFLSRF
TSLSAAALGN HLRLIRRLSI LVLLLMSWGM HRAITGVAPL ASIGLLSFAA AAQLAPALIG
ALYWRRAHRL GVLAGLVAGY GLWFYCLVLP AVFPQHVLLT DGLFGLQWLR PQQLFGLTLL
DPLSHGVLWS LLINILLFAA VSLLCRPRER DIRQAQAFVE LSELDRGADL ELTAIGVGQL
KSLMQPFVGL ERLEQIWSGF EQRSGQRLLA DDAVPRFAVA EAESILAGIV GSATAHQVMD
LLRANRPFQL EDIARLVDGT SQKLRFSQEL LQTTVETLSQ GISVVDADLR LVAWNQHYIE
LFDYPPRLLY IGCPVEKLYR HNAERGLYGK GVDIEVEIER RLQLLRHGSA HRFERRLPNG
TIVEVRGTPM PGGGFVTTFS DISDYRAAVD ALEENRRTLE ERVEQRTAEL RASNEALQAE
NRRRAEVEAQ MRELHAAKTR FLAHTSHDLL QPINAARLFI ASAQQKAGTG VSREMLEDIG
HIDSALGAAE QLIGALREIS RLDSGNLTPK YEHFAVGELL DALTVECQAI AASRGLQLRY
VRSAAWVYSD RHLLRRILQN FLSNALRYTV RGKVLLGARR RGRELEIQVW DTGPGIACEV
QEKIFEEFVR LSSADRPADK GLGLGLAIAK RSADLLRHPI RVRSTPGRGA VFSIRVPLGV
ALADKPKAPQ PRIAGADLSG IRVLCIDNED SILRGMQSLL SGWGCRVSAA RSLQEALSVW
PGTQPPQLVI VDYHLDCDAT GIGALEGLSE HWGQPLPGIL ISADISEQVR DAAVSRGYFY
LSKPVKPAAL RNLVRRLARR QPQAVDS
//
