ID A0A401HSP2_9BACL Unreviewed; 679 AA.
AC A0A401HSP2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PA598K_00250 {ECO:0000313|EMBL:GBF72020.1};
OS Paenibacillus sp. 598K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1117987 {ECO:0000313|EMBL:GBF72020.1, ECO:0000313|Proteomes:UP000288287};
RN [1] {ECO:0000313|EMBL:GBF72020.1, ECO:0000313|Proteomes:UP000288287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=598K {ECO:0000313|EMBL:GBF72020.1,
RC ECO:0000313|Proteomes:UP000288287};
RA Mizushima D., Miyazaki T., Shiwa Y., Kimura K., Fujita N., Yoshikawa H.,
RA Kimura A., Kitamura S., Hara H., Funane K.;
RT "A novel intracellular dextranase derived from Paenibacillus sp. 598K with
RT an ability of degrading cycloisomaltooligosaccharides.";
RL Submitted (MAR-2018) 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 -!- 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:GBF72020.1}.
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DR EMBL; BFBX01000003; GBF72020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401HSP2; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000288287; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR010808; CheA_P2-bd.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR035891; CheY-binding_CheA.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF07194; P2; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF55052; CheY-binding domain of CheA; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000288287};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 296..546
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 548..679
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 679 AA; 73798 MW; FAED1F51F2C632C4 CRC64;
MDMNAYLSMF IDESNDHLQS LNENLLRLEN EPEDLSIVQV IFRSAHTLKG MSATMGFEDL
ASLTHEMENV LDLVRNSKLK MDNFIFDTLF KGLDALESMV QDIVGGGTGK ADVTAIVQAL
QSIVKGDYSK PAESAGAAGN TAAGGGSGGL DEFQTSIMQQ SMESGHNVYH IQVTVREDCV
LKAARAYMVF DVLERGGEVI KSEPSVEQLE QEKFDREFIV FYISQLSAEE LQTQIQTVSE
IESASVTLLD AESLSLLAKP SLPASPQPQE IEASAEAVGQ VAAARSQSAA TAAPAAVSRT
IRVDIDRLDT LMNLFSELLI DRVRLEQLAG EIRRNDLIET VEHMARVSGD LQNIVLKLRM
VPVDSVFNRF PRMVRDLAKS LDKKIDLVIA GAETELDRTV IDEIGDPLVH LIRNSLDHGI
EQVADRTAAG KPETGTVHLR AYHSGNHVFI EIEDDGKGIN RDTVLKIAIK NGVIAPEQAD
SMSDEEVYML LFAAGFSTAD KISDISGRGV GLDVVKSKIS SLGGHVSVTS TLGKGTRFSI
QLPLTLSIIS AMLIKLGSEK YAVPLSSIVE TAIIKRESIR NIHGNRMIEF RGAIIPILSL
SRILESPDFS EDQEEESEVV IIRKGEKWAA VIVDDFIGQS EIVLKSLGNY LTGIEAVSGA
TILGDGQVAL IIDPNALIK
//
