ID   SMC_CLOK1               Reviewed;        1185 AA.
AC   B9E1H0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=CKR_1294;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; AP009049; BAH06345.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9E1H0; -.
DR   SMR; B9E1H0; -.
DR   PRIDE; B9E1H0; -.
DR   EnsemblBacteria; BAH06345; BAH06345; CKR_1294.
DR   KEGG; ckr:CKR_1294; -.
DR   HOGENOM; CLU_001042_2_2_9; -.
DR   Proteomes; UP000007969; 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..1185
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409268"
FT   DOMAIN          534..644
FT                   /note="SMC hinge"
FT   COILED          174..376
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          412..526
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          679..1039
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   1185 AA;  136916 MW;  5DB7862A8C1EB59E CRC64;
     MSMFLKTIEI KGFKSFADKT ELIFTGGITS IVGPNGSGKS NISDAVRWVL GEQSVKTLRG
     GKMEDVIFAG TQFRKPLGLC QVSLTLDNED KKLSLEYSNI TVSRRLYRSG ESEYYINNVQ
     CRLRDIHELF MDTGIGREGY SIIGQGRIDA LLSGKQEDRR LLLEEAAGIV KFRWRRSEAE
     KKLENTEVNL IRIEDILHTY EERLKPLELE NKKADEFLRL SEELKDKEKT VLIYSLKKIQ
     HKIDKLESSM ERITSSNRES HLELTKLRED VNGYNIRMEN IMDESTRCEK DYYDKRELIN
     QGENKIKLLK QKIEDLEDNI KRNYLELKQI ENDKIKKSEG ITLQNQNLLE LKNREKEVNI
     GILDYENNIK KIEKDIYSRE NICKKLKEDK IQYFSNISKL RNHIISIKKD GENIVEKIDK
     LKSSYESYSK AIIISSEKKN KLLGEISNIK KNISVYQNKI DENNSGILEL TNVLNLKENS
     LQKLNALYNT LEANYKMLVN FHKHYEGYNR TVKALMENIK NHKLDVPAQS CFLVGEIISL
     QKKFETCIEI SLGNSISSVI TNNEIIAKII IKYLKDNKMG RATFLPISII KGRKISNLHK
     FEDIKGFIGV ASELVSYSKE FKDVLDYILG RTIICENIDN AFEIAKLAEY SFKIVTLSGD
     VVNSGGAITG GSLQKRSSNI IGRKREIEET LVKIENTKET LQVLNGDIRR IKSDKEKLHC
     QNEDFKEKIH LDNIELTKLH QQNDTIERET KKLIESRETA NREIKLLYKN KEVNLNELQE
     EEKKLKEYSK EEIKNDDYIL KMEEELKEGR NRITDLKEGL TSLKVKRAQI SENILSSERE
     LSRLDQEIKS MDIKNRSIVE EIKLSEKIIH KNELNMYSNE KEVKDLKQYM EKLQESIEKS
     HVKTIELKQK INVSNEKVDN LTLIINKKET SFHKIQLELT KLNSQKDNIY SRLKEDMNIT
     CDGDIEYDVQ IENLEEYKSK IVHLKSSISK LGVVNLGAIE EYKNLQKKIT FLSSQKEDLI
     KSKQELKKVI DAMTEKMKGV FKENFVKLKK NFNDTFRELF KGGSADLVLT KGDELTGNID
     ITVQPPGKKL QNINLMSGGE KGLSAIALLF AMLKIKPTPF CILDEIEASL DDANVLRYAE
     FLRKFSRDTQ FIVITHRKGT MEVSDVLYGV TMEEKGVSKI ISLKL