ID   SMC_THASP               Reviewed;        1208 AA.
AC   C4ZJU1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=Tmz1t_2192;
OS   Thauera sp. (strain MZ1T).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=85643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT   "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL   Submitted (MAY-2009) 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 hinge near
CC       the middle of the molecule. These domains are separated by coiled-coil
CC       structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC   -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01894}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACK54932.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001281; ACK54932.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C4ZJU1; -.
DR   STRING; 85643.Tmz1t_2192; -.
DR   EnsemblBacteria; ACK54932; ACK54932; Tmz1t_2192.
DR   KEGG; tmz:Tmz1t_2192; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_4; -.
DR   OrthoDB; 1149850at2; -.
DR   Proteomes; UP000002186; Chromosome.
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; IPR011890; SMC_prok.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1208
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409283"
FT   COILED          170..205
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          239..504
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          694..1054
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   1208 AA;  133390 MW;  79E8058601A94DE7 CRC64;
     MRLSKLKLAG FKTFVDPTTV LTPGNLVGVV GPNGCGKSNI IDAVRWVLGE TRASALRGES
     MQDVIFNGST TRKPVSRASV ELVFDNAEGR AAGQWSRYAE ISVKRVLDRS GESTYYINNV
     HVRRKDVIDL FLGTGLGPRA YAIIEQGMIS RIIEARPEEI RGFLEEAAGV TKYRERRKET
     EGRLRDARDN LARLDDIRME LGERIVHLEA QAAVAARYRE LDAAHVEKQQ LLWLVKRNEA
     RAEQARVAAS LNEASSRIEA DSARLQELET SVESRRDAHF EASEAVHVAQ NDLFAASAEV
     ARLETELQHL GEARRRLEAR LAQLELDRGH WSSRRETLAA DRARWQELAE NAALRAEHAE
     ARHLEIADRL PELDSSRQGA DATMAAARRE LAQTEQQLRV EETKRASALR ALEALQQRRG
     RLEGERGGIV GPDERVLAER EARLEALQDE LEVHQQELAA AQPRLPDAQA ALKAALEHER
     AVQRRLTELR ARRDALMQLQ ARVQSQGKLG DWLERHGLDQ LPPLWKQLQV AAGWDEAVQA
     VLRERLAALT SPDPALALAA ARTVLDETPP ESLAIALPAR SGAPAERANC AQGPLSPQGR
     VTVATTATES STAIATDVAP AVLALAGLVE VRDPALRALV DDFLAGAWAV ERLEDWLPLR
     AQLAPSTCLV GPRGQVLTRD ALVHHAPDAR THGVIERQRE IEGLSAELQA HEDEAHLAHD
     ALVVAESAAS ALQERINGLR RELQTIQAQV HAEQVEVLKL AQARARAQER REQLARDLED
     IVHLESAERE HLTRAELEQA RAAELAELQR ERLDAATEVL REREHAVREA RALEQSAARE
     LQEARFSERE CAGKLEDIAR NQQLAGEQLE RVVAELAARA AELDATDDHR SAEALQEALA
     LRGRREAALA ARRDALAEAA AALKQVEELR LRTEHEAAPI RARVAELRLA LQAAELAVAQ
     FEERLVEARA DEAALAPLLA AEPKESTLQR EVARLAREIA ELGAVNMAAL DELTTASERK
     GYLDAQTEDL LQAIDTLEDA IRRIDRETRE QLQDTYNTVN RQFGALFPQL FGGGRAELVL
     TGEEILDAGI QIVAQPPGKK NASIHLLSGG EKALTAIALV FSMFQLNPAP FCMLDEVDAP
     LDDTNTERYA NMVKRMSAQT QFIFISHSKI TMEFAQQLVG VTMQEQGVSR VVEVDIEEAL
     RLADPAAA