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Database: UniProt
Entry: H8G3U3_9PSEU
LinkDB: H8G3U3_9PSEU
Original site: H8G3U3_9PSEU 
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
//
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