MCM_SACS2
ID MCM_SACS2 Reviewed; 686 AA.
AC Q9UXG1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Minichromosome maintenance protein MCM;
DE EC=3.6.4.12;
GN Name=MCM; OrderedLocusNames=SSO0774;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF LYS-346.
RX PubMed=11821426; DOI=10.1074/jbc.m200091200;
RA Carpentieri F., De Felice M., De Falco M., Rossi M., Pisani F.M.;
RT "Physical and functional interaction between the mini-chromosome
RT maintenance-like DNA helicase and the single-stranded DNA binding protein
RT from the crenarchaeon Sulfolobus solfataricus.";
RL J. Biol. Chem. 277:12118-12127(2002).
RN [4]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-318; ARG-331; LYS-346; ARG-359;
RP LYS-366; THR-374; ASP-404; 423-GLN-GLN-424; ASN-448; ARG-473; ASP-488 AND
RP ARG-560.
RX PubMed=17964268; DOI=10.1016/j.molcel.2007.08.013;
RA Moreau M.J., McGeoch A.T., Lowe A.R., Itzhaki L.S., Bell S.D.;
RT "ATPase site architecture and helicase mechanism of an archaeal MCM.";
RL Mol. Cell 28:304-314(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-268, AND SUBUNIT.
RX PubMed=18417534; DOI=10.1093/nar/gkn183;
RA Liu W., Pucci B., Rossi M., Pisani F.M., Ladenstein R.;
RT "Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal
RT domain.";
RL Nucleic Acids Res. 36:3235-3243(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (4.35 ANGSTROMS) OF 7-601, CATALYTIC ACTIVITY,
RP SUBUNIT, AND MUTAGENESIS OF LEU-189; ASP-191; 202-GLU--VAL-204;
RP 326-GLU-ASP-327; ARG-329; ALA-416; ALA-420; 550-THR--PRO-554 AND
RP 555-ILE--ASP-557.
RX PubMed=19073923; DOI=10.1073/pnas.0808037105;
RA Brewster A.S., Wang G., Yu X., Greenleaf W.B., Carazo J.M., Tjajadia M.,
RA Klein M.G., Chen X.S.;
RT "Crystal structure of a near-full-length archaeal MCM: functional insights
RT for an AAA+ hexameric helicase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20191-20196(2008).
CC -!- FUNCTION: Presumptive replicative helicase. Has ATPase and DNA helicase
CC activities. The latter preferentially melts 5'-tailed oligonucleotides
CC and is stimulated by the SSB protein (single-stranded DNA binding
CC protein). The active ATPase sites in the MCM ring are formed through
CC the interaction surfaces of two neighboring subunits such that a
CC critical structure of a conserved arginine finger motif is provided in
CC trans relative to the ATP-binding site of the Walker A box of the
CC adjacent subunit. The helicase function is proposed to use a partially
CC sequential mode of ATP hydrolysis; the complex appears to tolerate
CC multiple catalytically inactive subunits.
CC {ECO:0000269|PubMed:11821426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:17964268, ECO:0000269|PubMed:19073923};
CC -!- ACTIVITY REGULATION: Inhibited by the cdc6-2 protein. The ATPase
CC activity is not stimulated in the presence of DNA molecules.
CC -!- SUBUNIT: Homohexamers. Forms a complex with SSB.
CC {ECO:0000269|PubMed:18417534, ECO:0000269|PubMed:19073923}.
CC -!- INTERACTION:
CC Q9UXG1; Q9UXG1: MCM; NbExp=9; IntAct=EBI-8081298, EBI-8081298;
CC Q9UXG1; Q9UXG0: ORF-c40_009; Xeno; NbExp=5; IntAct=EBI-8081298, EBI-8081318;
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; Y18930; CAB57529.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41071.1; -; Genomic_DNA.
DR PIR; H90226; H90226.
DR RefSeq; WP_009991364.1; NC_002754.1.
DR PDB; 2M45; NMR; -; A=605-686.
DR PDB; 2VL6; X-ray; 2.80 A; A/B/C=1-268.
DR PDB; 3F9V; X-ray; 4.35 A; A=7-601.
DR PDB; 4FDG; X-ray; 4.10 A; A/B/C/D/E=7-686.
DR PDB; 4R7Y; X-ray; 2.70 A; A/B=2-269.
DR PDB; 6WNZ; X-ray; 2.00 A; A/B=1-269.
DR PDBsum; 2M45; -.
DR PDBsum; 2VL6; -.
DR PDBsum; 3F9V; -.
DR PDBsum; 4FDG; -.
DR PDBsum; 4R7Y; -.
DR PDBsum; 6WNZ; -.
DR AlphaFoldDB; Q9UXG1; -.
DR BMRB; Q9UXG1; -.
DR SMR; Q9UXG1; -.
DR DIP; DIP-42884N; -.
DR IntAct; Q9UXG1; 1.
DR MINT; Q9UXG1; -.
DR STRING; 273057.SSO0774; -.
DR PRIDE; Q9UXG1; -.
DR EnsemblBacteria; AAK41071; AAK41071; SSO0774.
DR GeneID; 44129780; -.
DR KEGG; sso:SSO0774; -.
DR PATRIC; fig|273057.12.peg.774; -.
DR eggNOG; arCOG00439; Archaea.
DR HOGENOM; CLU_000995_6_0_2; -.
DR InParanoid; Q9UXG1; -.
DR OMA; NAYTCDR; -.
DR PhylomeDB; Q9UXG1; -.
DR BRENDA; 3.6.4.12; 6163.
DR EvolutionaryTrace; Q9UXG1; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA replication; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..686
FT /note="Minichromosome maintenance protein MCM"
FT /id="PRO_0000194128"
FT DOMAIN 291..495
FT /note="MCM"
FT MOTIF 472..475
FT /note="Arginine finger"
FT BINDING 340..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 189
FT /note="L->D: Predominantly monomeric and loss of helicase
FT activity; when associated with R-191."
FT /evidence="ECO:0000269|PubMed:19073923"
FT MUTAGEN 191
FT /note="D->R: Predominantly monomeric and loss of helicase
FT activity; when associated with D-189."
FT /evidence="ECO:0000269|PubMed:19073923"
FT MUTAGEN 202..204
FT /note="EEV->GGG: Loss of helicase activity."
FT /evidence="ECO:0000269|PubMed:19073923"
FT MUTAGEN 318
FT /note="F->A: No effect on helicase and ATPase activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 326..327
FT /note="ED->AA: Impairs helicase activity; when associated
FT with A-329."
FT /evidence="ECO:0000269|PubMed:19073923"
FT MUTAGEN 329
FT /note="R->A: Impairs helicase activity; when associated
FT with 326-A-A-327."
FT /evidence="ECO:0000269|PubMed:19073923"
FT MUTAGEN 331
FT /note="R->A: Loss of helicase and ATPase activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 346
FT /note="K->A: Loss of helicase and ATPase activity."
FT /evidence="ECO:0000269|PubMed:11821426,
FT ECO:0000269|PubMed:17964268"
FT MUTAGEN 346
FT /note="K->A: Sharp decrease in ATPase activity. Almost
FT devoid of helicase activity."
FT /evidence="ECO:0000269|PubMed:11821426,
FT ECO:0000269|PubMed:17964268"
FT MUTAGEN 359
FT /note="R->A: Loss of helicase and reduction of ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 366
FT /note="K->E: Loss of helicase and reduction of ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 374
FT /note="T->E: Reduction of helicase and gain of ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 404
FT /note="D->A: Loss of helicase and ATPase activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 416
FT /note="A->R: Predominantly monomeric and loss of helicase
FT activity; when associated with R-420."
FT /evidence="ECO:0000269|PubMed:19073923"
FT MUTAGEN 420
FT /note="A->R: Predominantly monomeric and loss of helicase
FT activity; when associated with R-416."
FT /evidence="ECO:0000269|PubMed:19073923"
FT MUTAGEN 423..424
FT /note="QQ->AA: Loss of helicase and ATPase activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 448
FT /note="N->A: Loss of helicase and ATPase activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 473
FT /note="R->A: Loss of helicase and ATPase activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 488
FT /note="D->A: No effect on helicase and reduction of ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT MUTAGEN 550..554
FT /note="TPDSP->GGGGG: Predominantly monomeric and loss of
FT helicase activity."
FT /evidence="ECO:0000269|PubMed:19073923"
FT MUTAGEN 555..557
FT /note="ILI->DSD: Exclusively monomeric and loss of helicase
FT activity, ATPase activity and DNA binding."
FT /evidence="ECO:0000269|PubMed:19073923"
FT MUTAGEN 560
FT /note="R->A: Loss of helicase and ATPase activity."
FT /evidence="ECO:0000269|PubMed:17964268"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2VL6"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 119..130
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 134..146
FT /evidence="ECO:0007829|PDB:6WNZ"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:6WNZ"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2VL6"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:6WNZ"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:6WNZ"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:2M45"
FT HELIX 621..637
FT /evidence="ECO:0007829|PDB:2M45"
FT STRAND 640..644
FT /evidence="ECO:0007829|PDB:2M45"
FT HELIX 645..655
FT /evidence="ECO:0007829|PDB:2M45"
FT HELIX 659..672
FT /evidence="ECO:0007829|PDB:2M45"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:2M45"
FT STRAND 682..685
FT /evidence="ECO:0007829|PDB:2M45"
SQ SEQUENCE 686 AA; 77428 MW; C3ECD380F272E77E CRC64;
MEIPSKQIDY RDVFIEFLTT FKGNNNQNKY IERINELVAY RKKSLIIEFS DVLSFNENLA
YEIINNTKII LPILEGALYD HILQLDPTYQ RDIEKVHVRI VGIPRVIELR KIRSTDIGKL
ITIDGILVKV TPVKERIYKA TYKHIHPDCM QEFEWPEDEE MPEVLEMPTI CPKCGKPGQF
RLIPEKTKLI DWQKAVIQER PEEVPSGQLP RQLEIILEDD LVDSARPGDR VKVTGILDIK
QDSPVKRGSR AVFDIYMKVS SIEVSQKVLD EVIISEEDEK KIKDLAKDPW IRDRIISSIA
PSIYGHWELK EALALALFGG VPKVLEDTRI RGDIHILIIG DPGTAKSQML QFISRVAPRA
VYTTGKGSTA AGLTAAVVRE KGTGEYYLEA GALVLADGGI AVIDEIDKMR DEDRVAIHEA
MEQQTVSIAK AGIVAKLNAR AAVIAAGNPK FGRYISERPV SDNINLPPTI LSRFDLIFIL
KDQPGEQDRE LANYILDVHS GKSTKNIIDI DTLRKYIAYA RKYVTPKITS EAKNLITDFF
VEMRKKSSET PDSPILITPR QLEALIRISE AYAKMALKAE VTREDAERAI NIMRLFLESV
GVDMESGKID IDTIMTGKPK SAREKMMKII EIIDSLAVSS ECAKVKDILK EAQQVGIEKS
NIEKLLTDMR KSGIIYEAKP ECYKKV
