RAMA_STRCO
ID RAMA_STRCO Reviewed; 636 AA.
AC O88039; Q53818;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ABC transporter ATP-binding protein RamA {ECO:0000303|PubMed:15277670};
GN Name=ramA {ECO:0000303|PubMed:8206859}; OrderedLocusNames=SCO6683;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=A3(2) / M130;
RX PubMed=8206859; DOI=10.1128/jb.176.12.3800-3811.1994;
RA Ma H., Kendall K.;
RT "Cloning and analysis of a gene cluster from Streptomyces coelicolor that
RT causes accelerated aerial mycelium formation in Streptomyces lividans.";
RL J. Bacteriol. 176:3800-3811(1994).
RN [2]
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 [3]
RP OPERON.
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.
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 [5]
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).
CC -!- FUNCTION: Probably involved in exporting SapB from the cell (Probable).
CC Expression of the ram locus (ramA, ramB and ramR) induces rapid aerial
CC mycelium formation in S.lividans (PubMed:8206859).
CC {ECO:0000269|PubMed:8206859, ECO:0000305|PubMed:15277670}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Probably part of the ramC-ramS-ramA-ramB operon.
CC {ECO:0000269|PubMed:12100547}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the ramC-ramS-ramA-ramB operon on
CC rich medium leads to an initially bald (no aerial hyphae) phenotype;
CC after 4 days develops a substantial aerial mycelium. No expression of
CC SapB, normal expression of chaplins. Wild-type mycelium on minimal
CC medium. A complete chaplin-negative plus ram-negative strain (deletion
CC of ramR or the ramC-ramS-ramA-ramB operon) leads to the complete loss
CC of robust aerial hyphae. {ECO:0000269|PubMed:17462011}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U03771; AAA21388.1; -; Genomic_DNA.
DR EMBL; AL939128; CAA19962.1; -; Genomic_DNA.
DR PIR; T35182; T35182.
DR RefSeq; NP_630758.1; NC_003888.3.
DR RefSeq; WP_011031101.1; NZ_VNID01000002.1.
DR AlphaFoldDB; O88039; -.
DR SMR; O88039; -.
DR STRING; 100226.SCO6683; -.
DR GeneID; 1102122; -.
DR KEGG; sco:SCO6683; -.
DR PATRIC; fig|100226.15.peg.6788; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_11; -.
DR InParanoid; O88039; -.
DR OMA; GMWRTQA; -.
DR Proteomes; UP000001973; 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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..636
FT /note="ABC transporter ATP-binding protein RamA"
FT /id="PRO_0000445441"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 45..322
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 354..585
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 589..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 386..393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 372
FT /note="D -> G (in Ref. 1; AAA21388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 65481 MW; 04CA52FE1135E079 CRC64;
MSPAAGAPGS GPGRRRLPAL DVRRFSPVRK SRPVPPRAPG RALEVLVLLC SVAAAVAAVA
QPLALGRTLD LLLRDGDAGW WLPLSAALLL GELLLDSATS LFTGRCNATW TASVRTRALR
GLLRTAPEHA RPYPPGDIGT RLTLNAADAG GAPAARAALA ASLITPLGAL VALALVDVWV
ALCVLTGLPA LALLLRSFAR DTGATVAAYQ RTQSLIASRL LEALEGADTI GAAGTGERER
ARVLAPLAEL AAQGRHMWAL HGRALGRSGV LVPLLTLAAT AVGGLRLAAG ELSVGDLLAV
GRYAQLTAGV GAAASLLGAI VRAREARRRT RELERMTATV YGTRRLPPNG PGELRLCGVR
VLRGGREVLR ADGVRVPGGS TVAVVGRSGA GKSVLAAVAG RLIDPDEGYV LLDGVRLDRL
THEALRTEVA YAFERPVLGE GTIAEAVADG ARRSSRERVR QAARAAGADG FVRRLPHGYD
TPLPRAPLSG GEHQRLGLAR AFAHAGRLLV LDDATSSLDT ATEHEVDLAL RRSVRPGTRL
VVAHRPSVAD RADLVLWLED GQVRAVGTHR ELWHTAGYRE VFGAGAGAGA GAGAGAGADA
GAGADAGPGP DSGAATAVGG SGPGPVRRPE PEEARP
