RAMB_STRCO
ID RAMB_STRCO Reviewed; 608 AA.
AC Q7AKE5; Q53819;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=ABC transporter ATP-binding protein RamB {ECO:0000303|PubMed:15277670};
GN Name=ramB {ECO:0000303|PubMed:8206859}; OrderedLocusNames=SCO6684;
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. Wild-type mycelium
CC on minimal medium. No expression of SapB, normal expression of
CC chaplins. A complete chaplin-negative plus ram-negative strain
CC (deletion of ramR or the ramC-ramS-ramA-ramB operon) leads to the
CC complete loss 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; AAA21389.1; -; Genomic_DNA.
DR EMBL; AL939128; CAA19963.1; -; Genomic_DNA.
DR PIR; T35183; T35183.
DR RefSeq; NP_630759.1; NC_003888.3.
DR RefSeq; WP_011031102.1; NZ_VNID01000002.1.
DR AlphaFoldDB; Q7AKE5; -.
DR SMR; Q7AKE5; -.
DR STRING; 100226.SCO6684; -.
DR GeneID; 1102123; -.
DR KEGG; sco:SCO6684; -.
DR PATRIC; fig|100226.15.peg.6789; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_11; -.
DR InParanoid; Q7AKE5; -.
DR OMA; AFTYLVQ; -.
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 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; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 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; PS00211; ABC_TRANSPORTER_1; 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..608
FT /note="ABC transporter ATP-binding protein RamB"
FT /id="PRO_0000445442"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 30..296
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 376..605
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 321..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410..417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 608 AA; 62531 MW; 3B21B2C16E1B2F9C CRC64;
MTSTEAGALR RLAPPARRFL AHRKGVLVRL ALWSLAESGQ AFLVGHAVAR SVDEGFLAGD
PRRGLLWLGV ALVAVLSGAR VVRGVFAQLA GVTEPLRDGL VRHAVDRSMA RAAPGGPGGT
DRAAVSRLTN QVEIARDSFA GLVLTLRSFV FTAAGALLGL LSLHPALLVV VLPPLAAGLA
LFLVTLRPMA AAQRRALAAD EALGEHAASA RAALRDLTAC GTGPGAERHG ADLVADAAAA
ARTLAGWAAV RTAALGVAGH LPVLALLVAV EWLRGHGVSV GALLGAFTYL VQSLLPALHT
LMTALGAAGS RLLVVLDRIL GPEPEPEPEP EPEPEPELGS GLEPEPEPAS EPESGPSTAS
ASAAAFAVHT AAAPAVELRS VTLSYGVRAE PVLDALDLRV APGEHLAVVG PSGIGKSTLT
RLVAGTLAPS RGEVRVAGRV VTGRPAAELA ALRVLVPQDA YVFSGTVGDN LAYLRTDPSP
AELDAAVEAF GLAPLVERLG GLDATVRPAE LSPGERQLVA LVRAYLSPAP LLLLDEATCH
LDPASEARAE KALAGRSGTL VVVAHRLSSA VRADRTLVLD GIRAQSGTHA ELLGRSPLYR
DLTGHWNS
