ID   SMC_THEAC               Reviewed;        1140 AA.
AC   Q9HK21;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=Ta0787;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
CC   -!- FUNCTION: Required for chromosome condensation and partitioning.
CC       {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 SMC hinge
CC       near the middle of the molecule. These domains are separated by coiled-
CC       coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01894}.
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DR   EMBL; AL445065; CAC11918.1; -; Genomic_DNA.
DR   RefSeq; WP_010901200.1; NC_002578.1.
DR   AlphaFoldDB; Q9HK21; -.
DR   SMR; Q9HK21; -.
DR   STRING; 273075.Ta0787; -.
DR   PRIDE; Q9HK21; -.
DR   EnsemblBacteria; CAC11918; CAC11918; CAC11918.
DR   GeneID; 1456341; -.
DR   KEGG; tac:Ta0787; -.
DR   eggNOG; arCOG00371; Archaea.
DR   HOGENOM; CLU_001042_2_2_2; -.
DR   OMA; HNKIAME; -.
DR   OrthoDB; 1023at2157; -.
DR   Proteomes; UP000001024; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 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   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; SSF52540; 2.
DR   SUPFAM; SSF75553; SSF75553; 1.
DR   TIGRFAMs; TIGR02169; SMC_prok_A; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1140
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409288"
FT   DOMAIN          502..619
FT                   /note="SMC hinge"
FT   COILED          160..484
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          660..990
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1140 AA;  129825 MW;  EA719065561B14E6 CRC64;
     MSSYIERIEA HNFKSFRRKK VINFTKGLNV ISGPNGSGKS NIGDMLLFVL GTKSIHAVRA
     DRLSDLVSKG SGNECSVSVT FRSDDGRSLV IERRLVIEDE PKSYYYVNGV RSRLSEIDET
     LASMGINFGT YSFVLQGDIN DFISYSGQER RKLIERISGV DQFDSEIERV KADIEAVSRN
     MEINQTIIDE KRQNLERLRT EKEKKERYDA LLKRKRDVEY TEILNRKNAM ERQKRTIEGQ
     ISDLTKEIAQ LEERRSDLEK RSEAIRIRRE DVAKRIDDLT SGEMNRVKTD LHSVEVDIAK
     IRGIIDEKNR NMEKLEETIA KYESERDSTD REIEDLDRQI EEKAKRKRAL EDRYADLKKR
     YDDLFSRAQA EAVDAAETRR KSKEYQEKID GLGREIEELK AAGSQMNADL AVLLQKKAAL
     EERKEDLDLK IRTSEWKAKE TSEDMGKYSR KYYDLKAKYD QINDRISDLK SEISEKEASA
     KIASSRVPEY VRNVKMLEES VEGVIGLVRD LISYGEKYVK AVESAGGGRL NAVVVKDDAV
     AKECIQILKD RKISPMTFLP LNKMRDPPAQ RDVGKISKDP GYLGILMDFV DFEDQYRSAV
     YYAIRDTILV QDIDAGRRLM GIFRLVTLDG DIFDPGGSIT GGYRNYASDY ASALRMQHDL
     EGMKIQLSSL MDDRSRIKRE MDQAFSEMSE ASRRTGEIMK EQEMLKKEAE RSREELKQVM
     DDISSTDRAI ADKKRMIDEN EKVIEQKTLD LHKYQEALND LYDRIDPEFF KNIGDLSNEI
     NEVRSEIDAV ASELNQITSR RDILSSERKH LEDQMIDTKL QENSIAAEID DLNGKKRELE
     EKAKKYQYAL NDLEGRYGNL SAQVREADKQ IREMENGIND AKASIDLKND LMNDLKVKAG
     ILEGNLSSIE RELSSYSGCE AVIGDLQAMR QEIERAIMDL GEINNAAPQQ YEDALKDLDD
     YEKKHEKLME EKKALEETTA MLNEKKREVF VKTFTDISEK MNYVYGIING GTAKLIMIGS
     DPLTSSVEVS VTPKDKATVK IQALSGGEKS VAALSFITAV QILMPSSIYF LDEVDMYLDA
     YNAENMIKMI SQNAGEAQTI VISLKSLVFS YASNAIGVTS VNGESFVFNG HFDGSPEAAP