ID   MTRB_MYCPA              Reviewed;         565 AA.
AC   Q93CB7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Sensor histidine kinase MtrB;
DE            EC=2.7.13.3;
GN   Name=mtrB; OrderedLocusNames=MAP_3359c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19698 / CIP 103963 / DSM 44133 / TMC 807;
RA   Urbanic K.W., Mutharia L.M.;
RT   "Identification and initial characterization of the mtrAB two-component
RT   signal transduction system of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC   -!- FUNCTION: Member of the two-component regulatory system MtrA/MtrB.
CC       Seems to function as a membrane-associated protein kinase that
CC       phosphorylates MtrA in response to environmental signals (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS05909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF410884; AAL10208.1; -; Genomic_DNA.
DR   EMBL; AE016958; AAS05909.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q93CB7; -.
DR   SMR; Q93CB7; -.
DR   STRING; 262316.MAP_3359c; -.
DR   EnsemblBacteria; AAS05909; AAS05909; MAP_3359c.
DR   KEGG; mpa:MAP_3359c; -.
DR   eggNOG; COG5000; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_18_11; -.
DR   OMA; NRFWRSD; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..565
FT                   /note="Sensor histidine kinase MtrB"
FT                   /id="PRO_0000074808"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          235..287
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          302..519
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         305
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   565 AA;  61073 MW;  6D10AA571A4B50A7 CRC64;
     MMWGSRRRTR SRWGRSGPMT RGMGAVSRAV GTAWRRSLQL RVVALTLGLS LAVILALGFV
     LTSQVTNRVL DVKVKAAIEQ IERARTTVGG IVNGEEARSL DSSLQLARNT LTSKTDSASG
     AGTAGTFDAV LMVPGDGPRA ATTAGPVDQV PASLRGFVKA GQASYQYATV HTDGFSGPAL
     IVGSPASSQV ANLELYLIFP LKNEQATIQL VRGTMITGGA VLLVLLAGIA LLVSRQVVVP
     VRSASRIAER FAEGHLSERM PVRGEDDMAR LAMSFNDMAE SLSRQITQLE EFGNLQRRFT
     SDVSHELRTP LTTVRMAADL IYDHSADLDP TLARSTELMV NELDRFESLL NDLLEISRHD
     AGVAELSVEA VDLRSTVQSA LSNVGHLAED AGIELQVELP AEEVIAEVDT RRVERILRNL
     IANAIDHAEH KPVKIRMAAD EDTVAVTVRD YGVGLRPGEE KLVFSRFWRA DPSRVRRSGG
     TGLGLAISIE DARLHQGRLE AWGEPGVGSC FRLTLPLVRG HKVTTSPLPM KPIPQPSPSG
     GQSPSTGPQH AKDRARQREH AERSL