ID A0A0M2VF64_9GAMM Unreviewed; 1183 AA.
AC A0A0M2VF64;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VT06_07760 {ECO:0000313|EMBL:KKO49134.1};
OS Arsukibacterium sp. MJ3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Arsukibacterium.
OX NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO49134.1, ECO:0000313|Proteomes:UP000034895};
RN [1] {ECO:0000313|EMBL:KKO49134.1, ECO:0000313|Proteomes:UP000034895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:KKO49134.1,
RC ECO:0000313|Proteomes:UP000034895};
RA Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J.,
RA Stougaard P., Glaring M.A.;
RT "Draft genome sequences of two protease-producing strains of
RT Arsukibacterium isolated from two cold and alkaline environments.";
RL Submitted (MAR-2015) 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:KKO49134.1}.
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DR EMBL; LAHP01000008; KKO49134.1; -; Genomic_DNA.
DR RefSeq; WP_046553730.1; NZ_LAHP01000008.1.
DR AlphaFoldDB; A0A0M2VF64; -.
DR STRING; 1632859.VT06_07760; -.
DR PATRIC; fig|1632859.4.peg.1609; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000034895; 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:UP000034895};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 825..1037
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1059..1175
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 763..818
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1110
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1183 AA; 131250 MW; D312E6A8404D64F7 CRC64;
MTAWTVALLA LLYVGGLFWI ANWGERHADD RLIRKYGGLI YSLALAVYCT SWTYYGAVGT
AVTRGWDYIP IYLGPILLFI FGQPFLFKLL YVSKKQNVTS VADFISARYG KRKNIAMLVA
IICLIVVVPY IALQLKAVAS SYQVLLGGDF SDTVDHWYQD SALLSAIAMA FFAILFGTRK
LHLTEQNRGV MVAIAFESVV KLFALLTLAI AVYVFILDKE QNMLRAFAAH ATDLQTQYTT
SSIVEFTTKT ILAMAAVFLL PRQFHVAFVE NVSHHHLRHA RRWFSGYLLL VTVVVVPIAV
AGMQMFPTML PQADSFVLLI PAQSGWNSLS AMVFIGGFSA ATSMIIISTL ALSTMISNDV
VMPSLLQTNS RKEMPHDYSM LIILVRRAMI LLVMGLSYFY YLIFARDYEL AETGLMAFAL
AIQLAPAVIG GLYWRRGNAW GVYAGLSLGL VLWFYTLMLP QLVNAGVINS DIMQQGLSGL
VWLSPTSMFG IELDSLSHGV LLSLGFNILA YLLVSMLTNV NLQDRLQAVA FVKPNLPIDH
QDTPARRIRI RNTDLKILLE RFVGSHRAKE CLVEFGRKQH ISLQLDDLPS VGLVEHVERE
LAGVIGAASA SAMVNAVLEG RQLGFEDVVT LFDDTTQAIQ FSRKILFSTL EHLSQGVSVV
DRELKLVAWN KAYLEMFSYP EGMVRVGRSV ADIVRLNAER GLCGPGNPDE HVDKRIMHME
KGTAHVFQRV RPDGRVIEMR GNPIPGGGFV TSFTDISEHV TAVQALAEAK QHLEDRVQER
TQTISDINHE LLAEVDRRRQ TEQQLLHAKA EAEEANASKT RFLALASHDI LQPLNAARLF
TAALNGAQEK VQQKAILCQL DNSLKASEEL ISTLLEIAKL DDGKLKPDVQ PVALQELLSQ
LADEYSLLAS QKGLRLTVRM ADDYVQTDAT YLRRILQNML SNAIKYTVKG RVLLGFRKRG
DKLILQVWDT GPGIVKHDLA RIFEDFYRID ATAKGQQGVG LGLGVVNRMA KLLGHSLTVR
SWPGKGTLFS ITLPLAKQPY RQVFPLPGQH VQRPLPGLTV VCIDDDAANL AALKVLLEQW
QIAEVSCFYD DAELLAYART APAPDVMLID YQLGQHLNGL DLYQQIKHYW GNVGGILVSA
SPQADLAALA KAAGLMYLAK PIKPAALRAS LNHFKMLKRS NLL
//
