MSIK_STRCO
ID MSIK_STRCO Reviewed; 378 AA.
AC Q9L0Q1;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Diacetylchitobiose uptake system ATP-binding protein MsiK {ECO:0000305};
DE EC=7.5.2.- {ECO:0000305};
GN Name=msiK {ECO:0000303|PubMed:18957589};
GN OrderedLocusNames=SCO4240 {ECO:0000312|EMBL:CAB77334.1};
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, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=18957589; DOI=10.1099/mic.0.2008/019612-0;
RA Saito A., Fujii T., Shinya T., Shibuya N., Ando A., Miyashita K.;
RT "The msiK gene, encoding the ATP-hydrolysing component of N,N'-
RT diacetylchitobiose ABC transporters, is essential for induction of
RT chitinase production in Streptomyces coelicolor A3(2).";
RL Microbiology 154:3358-3365(2008).
RN [3]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=30089751; DOI=10.1264/jsme2.me17172;
RA Iinuma C., Saito A., Ohnuma T., Tenconi E., Rosu A., Colson S.,
RA Mizutani Y., Liu F., Swiatek-Polatynska M., van Wezel G.P., Rigali S.,
RA Fujii T., Miyashita K.;
RT "NgcESco acts as a lower-affinity binding protein of an ABC transporter for
RT the uptake of N,N'-diacetylchitobiose in Streptomyces coelicolor A3(2).";
RL Microbes Environ. 33:272-281(2018).
CC -!- FUNCTION: Part of the ABC transporter complexes DasABC-MsiK and NgcEFG-
CC MsiK involved in N,N'-diacetylchitobiose ((GlcNAc)2) uptake.
CC Responsible for energy coupling to the transport system.
CC {ECO:0000269|PubMed:18957589, ECO:0000269|PubMed:30089751}.
CC -!- SUBUNIT: The DasABC-MsiK complex is composed of two ATP-binding
CC proteins (MsiK), two transmembrane proteins (DasB and DasC) and a
CC solute-binding protein (DasA) (Probable). The NgcEFG-MsiK complex is
CC composed of two ATP-binding proteins (MsiK), two transmembrane proteins
CC (NgcF and NgcG) and a solute-binding protein (NgcE) (Probable).
CC {ECO:0000305|PubMed:18957589, ECO:0000305|PubMed:30089751}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:18957589}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene severely affects the
CC ability of the mutant to utilize maltose, cellobiose, starch,
CC cellulose, chitin and chitosan, but not glucose. The null mutant lacks
CC (GlcNAc)2-uptake activity, but GlcNAc transport activity is unaffected.
CC Mutant shows defects in induction of chitinase production.
CC {ECO:0000269|PubMed:18957589}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AL939119; CAB77334.1; -; Genomic_DNA.
DR RefSeq; NP_628414.1; NC_003888.3.
DR RefSeq; WP_011029527.1; NZ_VNID01000031.1.
DR AlphaFoldDB; Q9L0Q1; -.
DR SMR; Q9L0Q1; -.
DR STRING; 100226.SCO4240; -.
DR TCDB; 3.A.1.1.33; the atp-binding cassette (abc) superfamily.
DR TCDB; 3.A.1.1.36; the atp-binding cassette (abc) superfamily.
DR GeneID; 1099680; -.
DR KEGG; sco:SCO4240; -.
DR PATRIC; fig|100226.15.peg.4303; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_11; -.
DR InParanoid; Q9L0Q1; -.
DR OMA; PRNMYDK; -.
DR PhylomeDB; Q9L0Q1; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR CDD; cd03301; ABC_MalK_N; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015855; ABC_transpr_MalK-like.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR040582; OB_MalK.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17912; OB_MalK; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Sugar transport; Translocase; Transport.
FT CHAIN 1..378
FT /note="Diacetylchitobiose uptake system ATP-binding protein
FT MsiK"
FT /id="PRO_0000447873"
FT DOMAIN 4..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 378 AA; 40396 MW; 535347B126C9B69E CRC64;
MATVTFDKAT RVYPGSTKPA VDGLDIDIAD GEFLVLVGPS GCGKSTSLRM LAGLEDVNGG
AIRIGDRDVT HLPPKDRDIA MVFQNYALYP HMSVADNMGF ALKIAGVNKA EIRQKVEEAA
KILDLTEYLD RKPKALSGGQ RQRVAMGRAI VREPQVFLMD EPLSNLDAKL RVSTRTQIAS
LQRRLGITTV YVTHDQVEAM TMGDRVAVLK DGLLQQVDSP RNMYDKPANL FVAGFIGSPA
MNLVEVPITD GGVKFGNSVV PVNRDALKAA SDKGDRTVTV GVRPEHFDVV ELNGGAAKTL
SKDSADAPAG LAVSVNVVEE TGADGYIYGT VEVGGETKDL VVRVSSRAVP EKGATVHVVP
RPGEIHVFSS STGERLTD
