ID A0A432W4L7_9GAMM Unreviewed; 1128 AA.
AC A0A432W4L7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 12.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CWE09_11075 {ECO:0000313|EMBL:RUO24400.1};
OS Aliidiomarina minuta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Aliidiomarina.
OX NCBI_TaxID=880057 {ECO:0000313|EMBL:RUO24400.1, ECO:0000313|Proteomes:UP000288293};
RN [1] {ECO:0000313|EMBL:RUO24400.1, ECO:0000313|Proteomes:UP000288293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MLST1 {ECO:0000313|EMBL:RUO24400.1,
RC ECO:0000313|Proteomes:UP000288293};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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:RUO24400.1}.
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DR EMBL; PIPL01000002; RUO24400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432W4L7; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000288293; 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; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000288293};
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..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 780..990
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1015..1128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 735..766
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1062
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1128 AA; 125189 MW; 209C4CA888BDE8BF CRC64;
MLGVGTVLLV ASLYLLLLFS IASRGERNPR HGQARPWRYT LALGVHCTTW AFYGTITQAA
YYGWWFAPTY AGAILVFIVA HQLQIKLLRV VKAQNLTSLA DFIGARYGKS QSLAAMAAII
SLLALIPYIA LQLRAVTASF AAVTGFDAQQ LPWFNDVSTL VALTMMGFAI LFGARRLSLS
EQHPGLMDAI AFESIVKLAA FLLVGIFCTY FLFDGVNDLF IQAASSTDTR IMLEGVPNGT
YVYITHMLLG ALSMFVLPRQ FQVIFIENSH ESELRTARWA FPLYLFAINF FILPIALAGG
LLVPEFSGTD TFMLALPIAA EQPLISLIAF IGGLSAATSM VIMATLALSI MIANDVITPL
LVRKEQAKKP LLTLTSDKIL LIRRITIAAI IALAYGYHQL TEAGLPLVSN GLIAMALLVQ
LAPAMLGGLL WKRATHSGVI AGLIAGTLCW VIFLLLPSLQ ESAPSISGQL EARLSNGILL
SLGVNLALYV LVSLLTRHSP REQVQSLSFT DPEGHYHEGP HQAQLTWGRL RELLARFVDQ
DDIQQLEKRL NTPLLTQPAD EWAPSGLIAQ VERELAGAIG SAASRLMFES LEHQPNLPIA
QVVNWATEAS RLYKFNRELL QASVENIPQG ISVIDDNLRL VAWNRRYLEI FNYPDGFISA
GMPVADLLRF NAERGLFGNK AQNELQKEVD KRLEYLKQGS AYRYQRAHAD SIIELQGNPM
PEGGFVTTYT DITLLVSAQQ ELQRINQELE ARVEERTQAL NHAKLAAEDA HQSKTKFFAA
ASHDLMQPFN AATLLCDMLA QQIDSSQKQL LNQIRQSLHN AEELLTMLLE MTKLESGHLK
AQIAPLPLQD IFNNLDSTFS VMAEDKGLTL KIRPTSAIVL SDRRLLQRVL QNLLSNAIRY
TRNGRILCGV RRRKDHILLQ VIDTGSGIPE DKLEIIFDEF QQLEDDGDNP GLGLGLAIVD
RMTRLLGIPV HIQSKLDRGT CFSLQIALYD WELNTQPEKS IRAQNEGDKF LQGTHIITVD
NDPQVLNAIS QILREWGAEV SAVSSVEQAT EIEKIADLLL VDYHLDHSET GIQVIQRLRE
QWQKAIPAII NSADHSEKIR EAVIAEQAHF IPKPVKTAAL RRLLKRYL
//
