ID   SMC_HALOH               Reviewed;        1185 AA.
AC   B8CW13;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=Hore_07250;
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562;
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA   Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL69482.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8CW13; -.
DR   SMR; B8CW13; -.
DR   STRING; 373903.Hore_07250; -.
DR   EnsemblBacteria; ACL69482; ACL69482; Hore_07250.
DR   KEGG; hor:Hore_07250; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_9; -.
DR   OMA; HNKIAME; -.
DR   Proteomes; UP000000719; 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; 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..1185
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409274"
FT   DOMAIN          521..639
FT                   /note="SMC hinge"
FT   COILED          167..494
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          677..1031
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   1185 AA;  137294 MW;  7C49A7170E1FB6AB CRC64;
     MFLKKLELKG FKSFAKPITI NFESPITAIV GPNGSGKSNI VDAIRWVLGE QSAKTLRGSR
     MADVIFAGSK DYKALNKASV TLYLDNQDKI LPLDVSTVKI SRKVNMDGQS DYYLNGKICR
     LKDIENLLMD TGLGKDTYSI VGQGKIDSII NSRPEKLREL FEEAAGISKY KSRKMDAEKR
     LEKTNHDLQR IEDLIWELEK QVGPLEKAAQ KAKKYRRLKE ELKVLEVNLL LDKWDKNLDR
     LSSFEEDEQL LIHKLKSLTN NLTESQEKLE SLQRTLKVKK DELSRLRDRY YRQKSKREEA
     ENTLCILEER RQGLSREKEN LNQEIKDLNL RREELTGRLD EIGSRLIELK EKIDNYNQNY
     ESKKVLLDEI KENLDREKQD LFFLRNNILD GNVELKDISS QFEQLKERGR HLEEEIKRIK
     TTRDKISSEY DALNEREDKL RTYLKSVDNK IEEKRSVLTD LKEEELNLQA RLEEAKKRFN
     RTRNKLNEKN SHLSILHEME DSLEGYYRGV KNILKARSKL TGIIGVVADQ IEVDKKYELA
     IETALGGRLQ NIIVKDDKSA RECVDYLKET KGGQATFLPV NMVNGRKVNF KNNQVKKVDG
     FLGIASSFVD CEDYLKPVIE YLLGRTIIST DLKSAIEIAR LRKRGFKIVT LEGDVINSGG
     AITGGSKNSN KKMLLSRSRK IEDLKKEVLK LQNSLGEDSK NLNQLENKLK EVLNKKEVIK
     NDIRDLEIEK NNYHKDLIRL EQEKTKLSER LEEIDEEFVD CHDRLGKNDA AKQKLEDKLK
     ALNDDFSLEK NEIENKEKRV EELEARHENI NDEITRLKIN LAQLNEKRES LRKEEEKSNK
     ELIELAEKNE EFKERYNKIL SEIKGINNKE GQLNELKVKL SGEIEKLKND LNLTEKEVEE
     KQQRIDMLQR EVSDLQTRLD KKKDEKHQIE LKITRLENRN ERIVEILEND YDVKPEDGFD
     DRIKITNYSR AGQKVKELKN AIKKLGTVNQ GAIEEYNDLV DRLDYLQNQH DDLLKAKESI
     TKVIQEIEET MSSLFHEAFL KVNGEFNNTF KELFNGGQAS LKLTEPENLL ETGVEIVAQP
     PGKQLKKLSL MSGGERALTA IALVFAFLKV NPSPFYILDE IDAPLDDANV TRFARYIKEY
     SRFAQFLIVT HRKNMMAEAE TIYGVTMEES GVSKLISLKL SEQII