ID A7IBC4_XANP2 Unreviewed; 1170 AA.
AC A7IBC4;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Xaut_0058 {ECO:0000313|EMBL:ABS65317.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS65317.1, ECO:0000313|Proteomes:UP000002417};
RN [1] {ECO:0000313|EMBL:ABS65317.1, ECO:0000313|Proteomes:UP000002417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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; CP000781; ABS65317.1; -; Genomic_DNA.
DR AlphaFoldDB; A7IBC4; -.
DR STRING; 78245.Xaut_0058; -.
DR KEGG; xau:Xaut_0058; -.
DR eggNOG; COG0591; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_22_0_5; -.
DR OrthoDB; 9764438at2; -.
DR PhylomeDB; A7IBC4; -.
DR Proteomes; UP000002417; Chromosome.
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; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABS65317.1};
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:UP000002417};
KW Transferase {ECO:0000313|EMBL:ABS65317.1};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 813..1025
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1048..1163
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 758..806
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1099
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1170 AA; 126175 MW; 98CDAF5ED860E9EB CRC64;
MLRASVVIFA ALAYIGFLFA IASYGDRLRP KAARRAPRPM IYSLSLAVYC TSWTFFGSVG
LATTQGFDFL TIYLGPIILM TVGAPVFMRV VRLAKANNIT SIADFIAARY GKNQGIAALV
ALVAIVGAIP YISLQLKAVS ASLVAMLGHF AGEHGRGTVV GDLALFVACA MAAFAILFGT
RHTDATEHQD GLMLAIATES LVKLAAFLAV GIVVTFLIFD GPVELWYAAR EAGVTAPFEH
GFPLGNWLTM MVLSGGAFML LPRQFHVAVV ENKGEEEIHR ARWLFPLYLV LINLFVVPLA
LAGMTLFPLQ MVDSDVYVLA VPLAAGFDTI ALLAFVGGLS AATAMVIVES VAIAIMVSND
LVMPLLLRRR AAKADGGPPD DMTSVLLMVR RVAIFVIVLA AYLYHRITGD AQLAQIGLLS
FAAIAQVGPA FAAGILWQRA TANGAIAAIL TGSALWAYTL LLPSLAEAGL ISSTVVQNGP
FGLWLLKPTA LLGLSATPLA HGVAWSLGIN TLVLVVVSLL TQPSQIERVQ ARLFAGGGDR
GQMRPAFLRW RSSVTLGEVM ATVERYLGAE RARAAFENYA RQHGFILDPH READAGMVRY
AEHLLASAVG AASSRIVLSL LLRKRTVSTK AALKLLDDAS AAIQYNRELL QSAIDHVRQG
IAVFDRDLRL VCWNRQFGQM LDLPAECYAV GVPLTDILAS APADDEAKGS AAGVGARIAR
YAHPSPDFSE RLHQRGAVIE ARSDAMPDSG IAVTFTDITA SVEAALALER ANENLERRVR
ERTEELERLN GALEKAKAEA EEANLSKTRF LAAASHDILQ PLNAARLYVT TMVERARGPE
EERLAGNVDA SLESVEEILS ALLDISRLDS GVMRPEIAPF RIADILKPLE MEFAPLAREK
NLQLTFVPCS LAVRSDRRLL RRLLQNLISN AVKYTPHGRV LVGCRRHAGR LRVEVHDTGV
GIPRSKYKVV FQEFQRLDQG AKVARGLGLG LSIVERIARV LEHKVDVTSQ PSKGSTFSVD
LPVAVSMPEE PQAVPAPTRR GAQLDGLTVL AIDNEPAILE GMELLLKGWG CEVITASSAA
GALEAVRLTR KMPDVALVDY HLDDGHGIDA VMSLRWKLGK LPAVLITADR SKKVRDAARA
ADMEILSKPL KPAALRALLA HWRLARSAAE
//
