RAMC_STRCO
ID RAMC_STRCO Reviewed; 930 AA.
AC O88037;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable SapB synthase {ECO:0000303|PubMed:15277670};
DE EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=ramC {ECO:0000303|PubMed:15277670}; OrderedLocusNames=SCO6681;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LYS-285; ASP-395; ASP-413 AND ASP-438.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12169618; DOI=10.1128/jb.184.17.4920-4924.2002;
RA Hudson M.E., Zhang D., Nodwell J.R.;
RT "Membrane association and kinase-like motifs of the RamC protein of
RT Streptomyces coelicolor.";
RL J. Bacteriol. 184:4920-4924(2002).
RN [3]
RP FUNCTION, INDUCTION, OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=A3(2) / J1501, and ATCC BAA-471 / A3(2) / M145;
RX PubMed=12100547; DOI=10.1046/j.1365-2958.2002.03004.x;
RA O'Connor T.J., Kanellis P., Nodwell J.R.;
RT "The ramC gene is required for morphogenesis in Streptomyces coelicolor and
RT expressed in a cell type-specific manner under the direct control of
RT RamR.";
RL Mol. Microbiol. 45:45-57(2002).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=A3(2) / J1501;
RX PubMed=12453210; DOI=10.1046/j.1365-2958.2002.03255.x;
RA Nguyen K.T., Willey J.M., Nguyen L.D., Nguyen L.T., Viollier P.H.,
RA Thompson C.J.;
RT "A central regulator of morphological differentiation in the multicellular
RT bacterium Streptomyces coelicolor.";
RL Mol. Microbiol. 46:1223-1238(2002).
RN [5]
RP FUNCTION.
RC STRAIN=A3(2) / J1501;
RX PubMed=15277670; DOI=10.1073/pnas.0404220101;
RA Kodani S., Hudson M.E., Durrant M.C., Buttner M.J., Nodwell J.R.,
RA Willey J.M.;
RT "The SapB morphogen is a lantibiotic-like peptide derived from the product
RT of the developmental gene ramS in Streptomyces coelicolor.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11448-11453(2004).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=A3(2) / M600;
RX PubMed=17462011; DOI=10.1111/j.1365-2958.2007.05674.x;
RA Capstick D.S., Willey J.M., Buttner M.J., Elliot M.A.;
RT "SapB and the chaplins: connections between morphogenetic proteins in
RT Streptomyces coelicolor.";
RL Mol. Microbiol. 64:602-613(2007).
RN [7]
RP INDUCTION.
RC STRAIN=A3(2) / M600;
RX PubMed=22486809; DOI=10.1111/j.1365-2958.2012.08041.x;
RA Gaskell A.A., Giovinazzo J.A., Fonte V., Willey J.M.;
RT "Multi-tier regulation of the streptomycete morphogenetic peptide SapB.";
RL Mol. Microbiol. 84:501-515(2012).
CC -!- FUNCTION: Required for aerial hyphae formation (PubMed:12169618,
CC PubMed:12100547, PubMed:12453210). Probably involved in processing the
CC precursor of SapB to its mature form (Probable).
CC {ECO:0000269|PubMed:12100547, ECO:0000269|PubMed:12169618,
CC ECO:0000269|PubMed:12453210, ECO:0000305|PubMed:15277670}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12169618};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expressed in substrate hyphae and very immature aerial
CC hyphae. Expression commences by 24 hours after germination, is maximal
CC at 36 hours and has disappeared by 72 hours; expression is higher in
CC wild-type strain J1501 versus M145 (at protein level). Requires bldD,
CC cprA and ramR for expression, deletion of bldM or bldN increases
CC accumulation of RamC (PubMed:12100547, PubMed:12453210). Probably part
CC of the ramC-ramS-ramA-ramB operon (PubMed:12100547, PubMed:12453210).
CC Transcribed from 23 to about 40 hours after germination, requires ramR
CC for expression (PubMed:22486809). {ECO:0000269|PubMed:12100547,
CC ECO:0000269|PubMed:12453210, ECO:0000269|PubMed:22486809}.
CC -!- DISRUPTION PHENOTYPE: Deletion of ramC leads to loss of aerial hyphae
CC and sporulation on rich or minimal solid medium after 4 days growth
CC (PubMed:12169618, PubMed:12100547, PubMed:12453210). Deletion of the
CC ramC-ramS-ramA-ramB operon on rich medium leads to an initially bald
CC (no aerial hyphae) phenotype; after 4 days develops a substantial
CC aerial mycelium. Wild-type mycelium on minimal medium. No expression of
CC SapB, normal expression of chaplins. A complete chaplin-negative plus
CC ram-negative strain (deletion of ramR or the ramC-ramS-ramA-ramB
CC operon) leads to the complete loss of robust aerial hyphae
CC (PubMed:17462011). {ECO:0000269|PubMed:12100547,
CC ECO:0000269|PubMed:12169618, ECO:0000269|PubMed:12453210,
CC ECO:0000269|PubMed:17462011}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Val-27 is the initiator.
CC {ECO:0000305|PubMed:12100547}.
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DR EMBL; AL939128; CAA19960.1; -; Genomic_DNA.
DR PIR; T35180; T35180.
DR RefSeq; NP_630756.1; NC_003888.3.
DR RefSeq; WP_011031100.1; NC_003888.3.
DR AlphaFoldDB; O88037; -.
DR SMR; O88037; -.
DR STRING; 100226.SCO6681; -.
DR GeneID; 1102120; -.
DR KEGG; sco:SCO6681; -.
DR PATRIC; fig|100226.15.peg.6786; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_014914_0_0_11; -.
DR OMA; GWRTMPY; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01260; LANC_like; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..930
FT /note="Probable SapB synthase"
FT /id="PRO_0000445440"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 256..516
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 501..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 395
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 262..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 285
FT /note="K->A: Does not restore aerial hyphae formation to a
FT ramC deletion."
FT /evidence="ECO:0000269|PubMed:12169618"
FT MUTAGEN 395
FT /note="D->A: Does not restore aerial hyphae formation to a
FT ramC deletion."
FT /evidence="ECO:0000269|PubMed:12169618"
FT MUTAGEN 413
FT /note="D->A: Does not restore aerial hyphae formation to a
FT ramC deletion."
FT /evidence="ECO:0000269|PubMed:12169618"
FT MUTAGEN 438
FT /note="D->A: Partially restores aerial hyphae formation to
FT a ramC deletion."
FT /evidence="ECO:0000269|PubMed:12169618"
SQ SEQUENCE 930 AA; 100077 MW; B556154C647E6CCB CRC64;
MTAATVRGGT PRDSVVSVSN RWEGAGVNKG YAVYCDADPY FYDAPHRTAD RTGAARSRYA
AASSPVPEGW QRHESGDWLA LRPADADLPA QGWKIHVSAC LDNAESVLDR VWRHCVDGGT
AFKFVPSRYL LHQRNAKYAD RAGSGKFVTV YPADEAEFER LVGELSELLA GEPGPHILSD
LRIGDGPVHV RYGGFTRRDC YDADGELRPA VSGPDGVLVP DLRGPVFRIP EWVDPPAFLR
PHLDARSAVT VTGMPYTVES ALHFSNGGGV YLARDTRTGA RVVLKEARPH AGLAADGADA
VTRLHRERRA LERLSGLACT PEVLDHRTVG EHHFLVLEHI DGKPLNTFFA RRHPLIEADP
GERRLAEYTD WALDVHARVE RAVAEVHARG VVFNDLHLFN IMVRDDDSVA LLDFEAAHHV
DEAGRQIVAN PGFVAPPDRR GVAVDRYALA CLRIVLFLPL TSLLAVDRHK AAHLAEVVAE
QFPVDRAFLD AAVEEITRVD GSTRVDGSTR ADETTRADET TRLDVTTRVH GAPDAARRPA
GPVAPVRPDD WPRSRDSMAA AIRASATPSR TDRLFPGDIA QFATAGGGLA FAHGAAGVLY
ALAESGAGRD EDGEQWLLER TKRPPSGMPL GFHDGLAGLA WTLERLGHRD RALDLAELLL
DQPLDHLGPD LHGGTAGLGL ALESLAATTG QAALHSAALH CAELAADGLP GGSVPADRVS
RGRARAGLLY GGAGRALLFL RLFERTRDSA LLDLARDALR QDLARCVRGA GGALQVDEGW
RTMPYLGAGS VGIGMVLDDY LAHRADEEFA RAANEIVAAA QAMFYAQPGL YRGVAGMVLH
LGRTTATAPG TGPRAVRRQL DALSWHAMSY RDRLAFPGEQ MMRLSMDLST GTAGCLLAVA
SVLGDAPAGL PFLPPPRRSG GPLTRPHQEP
