ID D7APA8_THEM3 Unreviewed; 1196 AA.
AC D7APA8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Tmath_1309 {ECO:0000313|EMBL:ADH61024.1};
OS Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CCUG
OS 53645 / CIP 108742 / A3).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH61024.1, ECO:0000313|Proteomes:UP000002064};
RN [1] {ECO:0000313|EMBL:ADH61024.1, ECO:0000313|Proteomes:UP000002064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11426 / CIP 108742 / A3
RC {ECO:0000313|Proteomes:UP000002064};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.;
RT "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii
RT mathranii str. A3.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002032; ADH61024.1; -; Genomic_DNA.
DR RefSeq; WP_012995313.1; NC_014209.1.
DR AlphaFoldDB; D7APA8; -.
DR STRING; 583358.Tmath_1309; -.
DR KEGG; tmt:Tmath_1309; -.
DR HOGENOM; CLU_001042_2_2_9; -.
DR Proteomes; UP000002064; 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; 2.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 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 NCBIfam; TIGR02168; SMC_prok_B; 1.
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; 1.
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}.
FT DOMAIN 525..643
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..499
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 678..1019
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1196 AA; 138747 MW; 9F166419C7DC02B2 CRC64;
MYLKKLELQG FKSFADKVTL NFEKGVTAIV GPNGSGKSNI SDAIRLVLGE QSIKSLRGSK
LEDVIFAGSE NRKPLGFCEI NLTLDNSDGY LPFDYTEVVI TRKIFRSGES EFFINKTPCR
LRDIYELFLD TGVGKEGYSI IGQGRIDEIL SAKPEDRRQI FEEAIGISKY RYKKEEAEKK
LAAANDNLIR LNDIVAELEK QLTTLETQKS KAEEFLKLHK EKRKVDISLY IQLAKKSMNQ
YDALKGKYEN LKSQLNVKKI HKINQEENLL YKEKEIHDLK QQLDSKKEEY HNKLREIEIV
SGKRELIVEK LRNLEETSEL YREELKKAVK REELLREELK RVESNVALLH LNKKELEEKL
KQFQEEYISV QKQQKDKIEE VEKAKEDIIE ILNSIADVKG KLSLNNSLKE EAISRQQNLR
KHIEEIQNRI EKLDKEKNKI VEELQILQKE LDKKNQQKIT EQQALQKIEN EIILKENNLK
IIKEQIERKR SRLSILEEMD KNYEGYSGTV RNLLKLSENI PSFKENIIGV VGELLEVENT
YSTAIEVALG SNVQNIVIKS SDKVAELIER LKKENLGRAT FLPLDLIRGR ILSQQESNIL
SERGVIGVAS KLIKYNDNLE EIFNFLLGRV IIVDTIENAV RLSKKYNQAY KIVTLEGEVI
NPGGSITGGS LKPKLQSIFK RKEEITKLKK EIDSLKNQQE IVEEEIRQKM NDKIHEEEQI
ELLNKEVSDI RYNITSNEQR RISLEKEIGN LLNQLESYTL EIGELKENVR NYQQEIDRFL
KELESLEKEK ERLDALINGF KEKNNKEEEN LAILDKEITA LKIEIAKIEQ KLQNELHNLK
DKRQEFDREK NNIVEKEKNI KEIESLKVNL SLDREKLQGE IYKLQQEVEK IQKDISSLED
NIFQEEEDLQ KRKEKFSILQ QEFTNINEEF HKVEMEMQRF QIEIDNIKNR LWEEYELTLD
RAFEEAEEGE ISKLRQRADH LTKAIKGLGN VNIDAIEEYK EVKERYDFLK SQMEDIIKAK
ESLISVIEEA NKIIKTKFKD GFEILQIQFK ETFRRLFGGG NAELILTDED NLLETGIEIK
AQPPGKKLQT LSLLSGGEKA LVAISLLFAM LIIKPTPFCI LDEIDAALDD ANVERFAEFL
KELSKDTQFI VVSHRKGTMM VADAIYGVTM QEKGVSKLLS LKLNTDDKIG GLVKHA
//
