ID   MSMS_METAC              Reviewed;         998 AA.
AC   Q8THF6;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Methyl sulfide methyltransferase-associated sensor;
DE            EC=2.7.13.3;
GN   Name=msmS; OrderedLocusNames=MA_4561;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   GENE NAME, FUNCTION, COFACTOR, HEME-BINDING, AUTOPHOSPHORYLATION,
RP   MUTAGENESIS OF CYS-656, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=23661702; DOI=10.1074/jbc.m113.476267;
RA   Molitor B., Stassen M., Modi A., El-Mashtoly S.F., Laurich C., Lubitz W.,
RA   Dawson J.H., Rother M., Frankenberg-Dinkel N.;
RT   "A heme-based redox sensor in the methanogenic archaeon Methanosarcina
RT   acetivorans.";
RL   J. Biol. Chem. 288:18458-18472(2013).
CC   -!- FUNCTION: Heme-binding sensor kinase component part of a two-component
CC       regulatory system involved in methyl sulfide metabolism. Does not act
CC       as a phytochrome-like photoreceptor. {ECO:0000269|PubMed:23661702}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000269|PubMed:23661702};
CC       Note=Heme-binding is redox-active and coordinates various ligands such
CC       as imidazole, dimethyl sulfide, and carbon monoxide depending on the
CC       redox state. The redox state of the heme cofactor influences on
CC       autophosphorylation activity: while reduced protein does not
CC       autophosphorylate, oxidized protein promotes autophosphorylation
CC       signal. {ECO:0000269|PubMed:23661702};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23661702}.
CC   -!- PTM: Autophosphorylates: autophosphorylation is dependent on the redox
CC       state of heme cofactor and is promoted upon reduction.
CC   -!- DISRUPTION PHENOTYPE: Cells constitutively synthesize MtsF.
CC       {ECO:0000269|PubMed:23661702}.
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DR   EMBL; AE010299; AAM07900.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8THF6; -.
DR   STRING; 188937.MA_4561; -.
DR   EnsemblBacteria; AAM07900; AAM07900; MA_4561.
DR   KEGG; mac:MA_4561; -.
DR   HOGENOM; CLU_339705_0_0_2; -.
DR   InParanoid; Q8THF6; -.
DR   OMA; HQHIRIT; -.
DR   OrthoDB; 16486at2157; -.
DR   PhylomeDB; Q8THF6; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR   GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF13185; GAF_2; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF55785; SSF55785; 3.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Heme; Iron; Kinase; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transferase; Two-component regulatory system.
FT   CHAIN           1..998
FT                   /note="Methyl sulfide methyltransferase-associated sensor"
FT                   /id="PRO_0000429051"
FT   DOMAIN          40..77
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          117..169
FT                   /note="PAC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          209..246
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          250..302
FT                   /note="PAC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          314..458
FT                   /note="GAF 1"
FT   DOMAIN          469..540
FT                   /note="PAS 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          609..752
FT                   /note="GAF 2"
FT   DOMAIN          783..998
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   BINDING         656
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MUTAGEN         656
FT                   /note="C->A: Reversible conversion between Fe(2+) and
FT                   Fe(3+) under different redox conditions protein kinase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:23661702"
SQ   SEQUENCE   998 AA;  113060 MW;  367ABBE51BB4133B CRC64;
     MIGVDMKLET LVNNGPAVIF LCRAETGWPV ETVTANIVRF GYSPKDFISG GLGYADIIYP
     ADLEIAVSQF FSYVEKDYIG KDLDYKVEYR EYKGEAGEHK RNGKGNIGKD RGGYDSFTQQ
     YRLLNKSGDV LWVEAEIKVL EEEEGKAGLF QVTVFDISRW KHTEKAMPAA LDTENELKRI
     INSGHVIVFL WRAEPGWPVD FVSENISELG YTPEDFTSGR IVYTDIIHPD DLDNVRAEVS
     KNTEEGRDYF SKEYRVLAKS GEVRYVDERT LIRRNEKGEI TCYQGILLDI TQRKEAEELI
     LSQNRVLERI ASGASLDEVL LLLVNYAEEM KPGLLCTVML LDREQKRLFY GACPSLPKLY
     SKAINGIQVQ VNSETAGTAA GTGKRVIVGN IMKDPFCEEC REIAQKVGLK ACWAEPIFSS
     GGEVLGVFTI YLRETRKPRE EELEFIRTNA YLAGIAIEHV QAADALKESE NRFRTIFDNI
     NDQLYIREPD GISYMDVNQV VVDRLGYSKE EILNMKAEEI IPSEYWASVR ENMQKIKAEG
     SRIFEAGAVC KGGTVIPLEV SARIIDYGGK KTIFSVSRDI TERKKAEVAQ RLNGSRLEAL
     VKLDQMAGAS LKEITDFARE EAVRLTGSKL GYLAFMDAYE STLVMHSWSD SAMEECSIED
     KQFVYPVKSM GLWGEAVRQR KPIITNDYPA PNPLKKGYPK NHVHLIRHLN IPVFDGKRIV
     AVAGVGNKEE NYDESDVRQL TLLMQGMWQL IQRKQLEEAL RTYSGELSRA NEELRSVNMM
     KTEFVEEMMF PEKAEYGEIM DYETLYAIDS QQQKAVNTFI HYSEKLRRLV DSLLYQSLEK
     AGKIDYSFEE TQLKDVLSDA FLNNVFLIGE KALEVKKEVS ASLSEIKGDR EKLTALFTAL
     IDHAIKFTPQ GGKLALEVKE EAGNVHIVIA DSGKGISKEL IPYLFDRLYQ VNDSITRRYQ
     GLESGLYICK NIVDAHKGEI WFESEEGLGN LMHVKLPK