ID   SMC_THEVB               Reviewed;        1168 AA.
AC   Q7ZAK1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=tlr1925;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; BA000039; BAC09477.1; -; Genomic_DNA.
DR   RefSeq; NP_682715.1; NC_004113.1.
DR   RefSeq; WP_011057762.1; NC_004113.1.
DR   AlphaFoldDB; Q7ZAK1; -.
DR   STRING; 197221.22295651; -.
DR   EnsemblBacteria; BAC09477; BAC09477; BAC09477.
DR   KEGG; tel:tlr1925; -.
DR   PATRIC; fig|197221.4.peg.2014; -.
DR   eggNOG; COG1196; Bacteria.
DR   OMA; HNKIAME; -.
DR   OrthoDB; 1149850at2; -.
DR   Proteomes; UP000000440; 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; 1.
DR   SUPFAM; SSF75553; SSF75553; 1.
DR   TIGRFAMs; TIGR02169; SMC_prok_A; 1.
DR   TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1168
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409284"
FT   DOMAIN          521..634
FT                   /note="SMC hinge"
FT   REGION          330..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          166..508
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          673..790
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          820..1011
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1168 AA;  133129 MW;  6FBC998A2DB04D1D CRC64;
     MYIKRLELTN FKSFGGTTVI PLLPGFTVIS GPNGSGKSNL LDALLFALGL AGSKGMRAER
     LPDLVNHSQT RRGHSVVETR VTVTFALDAE TEWRVTRRLR VTKQGSYTST YAVNDQPCTL
     NELHDQLQAF CIYPQGYNVV LQGDVTSMIS MNAKARREII DELAGVADFD RKIAQAREKL
     DTVKEREERF RIVERELIQQ RDRLQRERLH AEKYQALRLE LQEREQWLLV RQWQAHEEQK
     VQLQAQIQTL QQEQTQRQEQ LQQKAQEMAA AAVTLEQLNR QVKALGEEEY LRLQATLADL
     HAQQRQCQRQ QAANQQQQEQ LAEQLQQGQA QYHRQQAQHR QLAEELAQQR GDRTPLMTAV
     ANSQATLEAL RQQVQELSTA AQTWFQEHSQ RRQRIDALIH ELEPSRTELS RLQERSQQLR
     QRQGELHQAA TALEGQQLEL QDALTTAAAA IKQQEQQLQT LAQQLATAQQ QLSRTEETYQ
     RLEREQRQKQ RELDQLEARQ QAVQETQGGF AARLILSADL PGVLGLVAQL GQVEPRYQLA
     LEIAAGARLG NIVVADDSVA AAAIALLKRE QAGRATFLPL NKMARPKPLS PIALAGCIDY
     ALNLVTFEPQ YAPIFAYVFG STLVFESLEA AREYLGQYRM VTLEGELLEP SGAMTGGSQR
     RPNTLRFAQG VPPQESAEVQ QVRDRLGELE RLLDRLLQER THQQGRVNAL SQALSEAHQS
     HRDRQRQWEQ LQQQQQQLNR QQAELERQQQ YLSQELTAAE TELTHLEARL PELEAELAAE
     RLALNALEAS PSHQQWQQVQ AQLQAQEKIH ASQVAALQAV DQALGDRHRQ LEQLERDLKQ
     TEQEIQRLCQ AQREMRCQQQ ALDQTLGDLA TQIERTQAAL RELDSRLGHL KGDRDRHEYQ
     LRQQQKNYQQ LEWQYQKASE TLTTLQAQLQ ELSTIEPPPL PQPLPEVPAE LSLRDIQQQC
     QALEQRLRAM EPVNMLAIQE FEETQARLKE LQEKLAVLAA ERTEILLRIE NFTTLRHQSF
     REAFDAINAN FQTIFATLSD GDGYLQLESP EDPFAGGLNL VAHPKGKPVQ RLASMSGGEK
     SLTALSFIFA LQRYRPSPFY AFDEVDMFLD GANVERLAKM IQQQSQQAQF IVVSLRRPMI
     EAAQRTIGVT QARGQHTQVI GLDLTAYP