ID   SMC_DESHY               Reviewed;        1198 AA.
AC   Q24U48;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=DSY2655;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE84444.1; -; Genomic_DNA.
DR   RefSeq; WP_011460497.1; NC_007907.1.
DR   AlphaFoldDB; Q24U48; -.
DR   SMR; Q24U48; -.
DR   STRING; 138119.DSY2655; -.
DR   EnsemblBacteria; BAE84444; BAE84444; DSY2655.
DR   KEGG; dsy:DSY2655; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_9; -.
DR   OMA; HNKIAME; -.
DR   OrthoDB; 1149850at2; -.
DR   Proteomes; UP000001946; 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;
KW   Reference proteome.
FT   CHAIN           1..1198
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409271"
FT   DOMAIN          534..647
FT                   /note="SMC hinge"
FT   REGION          785..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          175..211
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          322..524
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          687..1042
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COMPBIAS        800..818
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1198 AA;  135528 MW;  010E450212493253 CRC64;
     MAKADTLPVF LKSITIQGFK SFADKVKLEL GQGLSVVVGP NGSGKSNVAD AIRWVLGEQS
     AKNLRGSKME DVIFSGSSVR RPVGMAEVSL FFDNSTGIFP LEYQEVIITR RVYRDGEGQY
     FINRSSCRLK DIHELFMDTG AGKEGFSIIG QGRVEEILNL RSEERRTLIE EASGITKYRM
     RKREALKRLD ETEHNLERIR DILAEIEGQL GPLEEQATIA REAVELTTEQ KALEIEIVAF
     DLKEVRHKLT TSVQETEELQ SAIAAAVADL SQKESEILGN KVKLNLLDEQ IQKQQETTYQ
     LDQAVNQIVQ ELRLRQEREG YLGEQINRVT TELSSHEEKV RQSTEQLRAL EDRKALLHKT
     LEQANQALAA DEQRLAEAKA RNGLEEIEIL RGSLSHLQSK LAESTAELNR FTHQLATLNS
     THEQLVKEKK DKEAALFSHE QQEAQVQEQL KAQEELQTDI RLQTERAHQE TAQLREQSKA
     GQRELQELNR DLEKKSARYH ALKNLEDSLE GYQRGVRELM LAKKKNQPSC GDLCGTLADL
     LQVEERYEVA VEVALGAGIQ NIVTETERGA KEAVHYLKSH NLGRATFLPL DVIQGGKATV
     AKEAAQDPGF IGVAVDLITF AEKYRKAFES QLGRTLIVTD MEAATRVARA SGYRARIVTL
     EGDQVHPGGS LTGGSLQRKG SNLLGRSREI QELRQECDER RTQQKEMELK AGALGTQIQK
     GEENLKHLMG EEQELKSALA VLRTQELNLR AQAQRIHEEV TAIAARMAGI EQERDELQSH
     KALGAEEQSK LTDSIQEAQE ALARQEEKNR QASREMEQLQ ERLTQTKVQA AKWEQELKQA
     VERLAQDQAL LGENKHLLER KRKDLQDLEE SKARLAFEQG DWESRRREAG EQQQQAQEVL
     IALRKEREVL SKELMDQESL AQKKRQEQQT LEQKLHNLEL KTARWDAEWE TGSRRLLEEF
     DLTWDEAQTY QSERNRAELG ARVQEIKLRM ELLGPVNQAA IEEYPKLQER YDFLSVQKQD
     LEEANESLQQ LIAELDKTMS ERFEEGFIAV NEAFKVVFKE LFNGGYAELR LVDPTNLLDT
     GVEIIAQPPG KKPQLLSLLS GGERALTAIG LLFALLKVKP SPFCVLDEIE ASLDDANVSR
     FAQYIHRLSD STQFLVISHR KGTMEAADVL YGITMEESGV SKLLSVQLEG QDKDTRTA