ID A6VQ25_ACTSZ Unreviewed; 660 AA.
AC A6VQ25;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Asuc_1720 {ECO:0000313|EMBL:ABR75072.1};
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR75072.1, ECO:0000313|Proteomes:UP000001114};
RN [1] {ECO:0000313|Proteomes:UP000001114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC {ECO:0000313|Proteomes:UP000001114};
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000746; ABR75072.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VQ25; -.
DR STRING; 339671.Asuc_1720; -.
DR KEGG; asu:Asuc_1720; -.
DR eggNOG; COG4192; Bacteria.
DR HOGENOM; CLU_020981_1_0_6; -.
DR OrthoDB; 9772100at2; -.
DR Proteomes; UP000001114; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR017116; Sig_transdc_His_kinase_PgtB.
DR PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PIRSF; PIRSF037119; STHK_PgtB; 2.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABR75072.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001114};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 354..406
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 451..658
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 660 AA; 76505 MW; 2D645C5982FE862F CRC64;
MRKWINSLNI SRGLQLSFWL SALLCLFVGG LGLLTWQQQR AEINIALSEN FPQVQSAFQA
EEQANLLHNA FIQFSNSKTT TEKVEFYQHT RKHLAALRTL LTVLKENLNK NLLLILTQQE
NLLERLSTTI SAQLTLNESF SHSLAKINWL NNDFKQEFTA LLQEIAWQQS TLAKNITHQS
SNERQLIQLH QLQQQLVLVN DFMQYEELLI HELSKQISDP DNHQEELFRN QLDYLSLLIQ
QRFEPLQLHA AGETIKQILN ELLALGLNKM QLPELFSRHK TLQQEKQQLI QQSNQLFQHF
RQTVREQVGN SKNQLDLLHN IVAKSTRFNG IIILAVMLFA FLLVIAVNYF YIRLRMLKRF
DRLNQAVAQL TQGEENVKIA VYGNDELGKI ARLLRLFLFE MQHKQLELSK RNQVLMDEIE
YRIKVQDELM QLQQELTQAA KLAVVGKTLT SISHEITQPL NAMNAYIFSA KRALQKQNYE
ATYDYLDKIN RLTEKTAVII KRLRQFSKQG NGKLQAVNLN ESFANAWELL ESKHKHRKVR
LDLPQNLPHI WGENVLIEQV FVNIFLNALE AIEQDPPQIK VEIQWQNSQE ICLWIIDNGR
GWPLSDKLLQ PFSSSKSLNL GLGLSISRSI MQQCGGELRI ASTLQRNALV ILIFKVAHHV
//
