ID H8G3U3_9PSEU Unreviewed; 901 AA.
AC H8G3U3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Signal transduction histidine-protein kinase/phosphatase MprB {ECO:0000256|ARBA:ARBA00040454};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Mycobacterial persistence regulator B {ECO:0000256|ARBA:ARBA00041776};
GN ORFNames=SacazDRAFT_02200 {ECO:0000313|EMBL:EHY89111.1};
OS Saccharomonospora azurea NA-128.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882081 {ECO:0000313|EMBL:EHY89111.1};
RN [1] {ECO:0000313|EMBL:EHY89111.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA-128 {ECO:0000313|EMBL:EHY89111.1};
RX PubMed=22768365; DOI=10.4056/sigs.2635833;
RA Klenk H.P., Held B., Lucas S., Lapidus A., Copeland A., Hammon N.,
RA Pitluck S., Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G.,
RA Land M., Ivanova N., Rohde M., Goker M., Detter J.C., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the soil bacterium Saccharomonospora azurea type strain
RT (NA-128(T)).";
RL Stand. Genomic Sci. 6:220-229(2012).
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; CM001466; EHY89111.1; -; Genomic_DNA.
DR RefSeq; WP_005441457.1; NZ_CM001466.1.
DR AlphaFoldDB; H8G3U3; -.
DR HOGENOM; CLU_002554_0_0_11; -.
DR OrthoDB; 3502710at2; -.
DR Proteomes; UP000004705; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 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; IPR013587; Nitrate/nitrite_sensing.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF9; SENSOR PROTEIN RSTB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08376; NIT; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHY89111.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 546..652
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 745..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 901 AA; 97812 MW; C0573E4DF4FDBABE CRC64;
MTRRSERPRD GAATAERAGG RWRVRNWRLR TKLVAILLIP AVAVLVLVAL RATDDLDRAA
TFSEGAERIR VETTVAEVVH QLQRERDLTV RHVAGGREGS LDELKEQRER VDAAIGEFDR
TLAGSAHALS PETLALFERI GQEFGTLTGL RYAGENTALP SEAVLRSYSD LISDVLGVGE
VFVSDAVDRE LAGSRLVANA LARVKDQLSI RRAVVAQALA RGSLTKDVER ALVSAEAQLA
AAKDDFTTFA TPRQRRMYDD TVIGLVVDLG NGIVESVLTR AENGGDLAGL SADEWDRAST
YTVNLVKRVQ EQLLEDLQER SDALAADARS SAGTDAGVVL GALLLGAILA VVVARSLLRP
LRALRSSALD VAEHKLPAAV DDILTEENPT PEHMYTRAVE PVPVHTRDEL GEVARAFDAV
HGEAVRLAGQ QAMLRENVNS MFVNLSRRSQ DLVERQLVVL DRMEEHEQDP EILGGLYELD
HLATRMRRNS ENLLVLAGED GGRPLPGSVP ASEIIGAALS EVEHYQRISV ETPPMLSVQG
DVASDLIHVI AELFENATAY SPEREMVTVV SSVTRERQWR IEITDRGAGM PETEIRRANT
RLAEPPDVDV EVSRRMGLYV VGRLARRHQI EVRLAAAEPR GLTATVLVPA EFVEPDNPES
IELPVPSTAS ASAEVPPASP VSHALGVAAN VHVEAVVEAD EDDWAGAPQP DEPAELDRLP
LLTHSLDEWT LEDDRLVGAT VFEPAELPDE TPRRTTVELG AQPAWPTEDD DARHPPALEE
EVPTDRLPAY QAVLSQWFPE TDIPGADEVS WPGEPTGPGE VVDDETDLER TEPTATGAGA
IASALADEED DTVPGPVAPR HGVVDRRGER PPPVNRSPEA VRARMASLQR GVQRGRHAGG
D
//