ID Q6MTD2_MYCMS Unreviewed; 988 AA.
AC Q6MTD2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=MSC_0476 {ECO:0000313|EMBL:CAE77104.1};
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632 {ECO:0000313|EMBL:CAE77104.1, ECO:0000313|Proteomes:UP000001016};
RN [1] {ECO:0000313|EMBL:CAE77104.1, ECO:0000313|Proteomes:UP000001016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1 {ECO:0000313|EMBL:CAE77104.1,
RC ECO:0000313|Proteomes:UP000001016};
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC each terminus and a third globular domain forming a flexible hinge near
CC the middle of the molecule. These domains are separated by coiled-coil
CC structures. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; BX293980; CAE77104.1; -; Genomic_DNA.
DR RefSeq; NP_975462.1; NC_005364.2.
DR AlphaFoldDB; Q6MTD2; -.
DR STRING; 272632.MSC_0476; -.
DR KEGG; mmy:MSC_0476; -.
DR PATRIC; fig|272632.4.peg.516; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_14; -.
DR Proteomes; UP000001016; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03278; ABC_SMC_barmotin; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 6.10.140.1720; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01894; Smc_prok; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR InterPro; IPR011890; SMC_prok.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 3.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000001016}.
FT DOMAIN 420..540
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 170..278
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 342..369
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 579..648
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 988 AA; 112935 MW; 8A9A7171FD733F50 CRC64;
MLFLKQIRAS GFKSFADLTV MDFNYDMTGV VGPNGSGKSN ITDAIRWTLG EQSTKTLRGS
KMDDIVFSGN NEKKAADVAE VTLVFNNIHE NFSSIKSDVV EITRKFDKNT RESEFYINST
KCKLKDVQSI ALEAGLTRSS IAIISQGTVA NFTESKPETK REIFDDAAGV SKYKKRKKET
LSKLEKATEN LTRLEDIAKE ISRRLPNLER QSKKALEYQQ KVNELKNIEL YILTKDLKVL
VNRIEELRVE KIEYETQIKK LTNEINMSQE EVNLIIDKDS EDNQKLGELN AKFNSIVEKI
ANLKVRKQKA KFKEQENLNT KDQDEYKAAL IKKQFDEKQI SIKSEKNKLT KAENSLLELK
DKYDYYSNKY NEIYREIETI RITISRISIQ IEAIEHNKKA ALQSYQDEVS AILNNQKQIG
GVVGVLKSLI NVKEEYQIAI SVTASGHMNS LVMKTDQDVK KAIEFLKKNN NLGRVTFLPL
NTLTPNLINP VQRQILEKSE GFVGFANELV EYSETISKAV EYALASIIVV QSYDDAINLA
KNTNFRFNIV SLDGQRILPR GAIVGGSTRN ANIFTKQNTQ NQDNNLEELK NKIELLEQKE
ISKTKEITEY KTANDSLRDQ INDLNGTIRN AKNNLFNWTE NLKEFSDEHK SLTGRDLFTG
VYSKSDESES IILAKQISEL EIQRDEIQIE INSISFKRNQ SMEKQKEMNS KNSKKRDELD
ELKTHAGSIN TEYNVLLQRR ITIIDRLSNG YQITEETALT MEVENIEDEQ VARERIIELT
TYIQNIGNVN MDAIEEYKNE KERFDYYDQQ IKDIYDAKEK LESIILDIDI AMESQFKQII
EDVNKTLPDV FSKMFGGGYA ELIYTDPDNI LETGIDIKIF PPGKKITNLN LLSGGEKSLV
ALSVLFAILK ARPLPLVILD EAEAPLDPVN VERFARYVRQ FSHNTQFIIV THREGTMTQC
DSLFGVTMQT KGITKIINVK LVEAKNLH
//
