ID   SMC_MYCTO               Reviewed;        1205 AA.
AC   P9WGF2; L0TCM4; Q10970;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=MT2990;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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; AE000516; AAK47317.1; -; Genomic_DNA.
DR   PIR; B70748; B70748.
DR   RefSeq; WP_003899542.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGF2; -.
DR   PRIDE; P9WGF2; -.
DR   EnsemblBacteria; AAK47317; AAK47317; MT2990.
DR   KEGG; mtc:MT2990; -.
DR   PATRIC; fig|83331.31.peg.3231; -.
DR   HOGENOM; CLU_001042_2_2_11; -.
DR   Proteomes; UP000001020; 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; TIGR02168; SMC_prok_B; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding.
FT   CHAIN           1..1205
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000428372"
FT   DOMAIN          514..628
FT                   /note="SMC hinge"
FT   COILED          169..288
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          330..499
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          661..771
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          802..836
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          979..1033
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   1205 AA;  130637 MW;  A3B2A813B58EACF3 CRC64;
     MYLKSLTLKG FKSFAAPTTL RFEPGITAVV GPNGSGKSNV VDALAWVMGE QGAKTLRGGK
     MEDVIFAGTS SRAPLGRAEV TVSIDNSDNA LPIEYTEVSI TRRMFRDGAS EYEINGSSCR
     LMDVQELLSD SGIGREMHVI VGQGKLEEIL QSRPEDRRAF IEEAAGVLKH RKRKEKALRK
     LDTMAANLAR LTDLTTELRR QLKPLGRQAE AAQRAAAIQA DLRDARLRLA ADDLVSRRAE
     REAVFQAEAA MRREHDEAAA RLAVASEELA AHESAVAELS TRAESIQHTW FGLSALAERV
     DATVRIASER AHHLDIEPVA VSDTDPRKPE ELEAEAQQVA VAEQQLLAEL DAARARLDAA
     RAELADRERR AAEADRAHLA AVREEADRRE GLARLAGQVE TMRARVESID ESVARLSERI
     EDAAMRAQQT RAEFETVQGR IGELDQGEVG LDEHHERTVA ALRLADERVA ELQSAERAAE
     RQVASLRARI DALAVGLQRK DGAAWLAHNR SGAGLFGSIA QLVKVRSGYE AALAAALGPA
     ADALAVDGLT AAGSAVSALK QADGGRAVLV LSDWPAPQAP QSASGEMLPS GAQWALDLVE
     SPPQLVGAMI AMLSGVAVVN DLTEAMGLVE IRPELRAVTV DGDLVGAGWV SGGSDRKLST
     LEVTSEIDKA RSELAAAEAL AAQLNAALAG ALTEQSARQD AAEQALAALN ESDTAISAMY
     EQLGRLGQEA RAAEEEWNRL LQQRTEQEAV RTQTLDDVIQ LETQLRKAQE TQRVQVAQPI
     DRQAISAAAD RARGVEVEAR LAVRTAEERA NAVRGRADSL RRAAAAEREA RVRAQQARAA
     RLHAAAVAAA VADCGRLLAG RLHRAVDGAS QLRDASAAQR QQRLAAMAAV RDEVNTLSAR
     VGELTDSLHR DELANAQAAL RIEQLEQMVL EQFGMAPADL ITEYGPHVAL PPTELEMAEF
     EQARERGEQV IAPAPMPFDR VTQERRAKRA ERALAELGRV NPLALEEFAA LEERYNFLST
     QLEDVKAARK DLLGVVADVD ARILQVFNDA FVDVEREFRG VFTALFPGGE GRLRLTEPDD
     MLTTGIEVEA RPPGKKITRL SLLSGGEKAL TAVAMLVAIF RARPSPFYIM DEVEAALDDV
     NLRRLLSLFE QLREQSQIII ITHQKPTMEV ADALYGVTMQ NDGITAVISQ RMRGQQVDQL
     VTNSS