ID   SMC_MESHY               Reviewed;         979 AA.
AC   P41508;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
DE   AltName: Full=Protein P115;
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894};
OS   Mesomycoplasma hyorhinis (Mycoplasma hyorhinis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=2100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1825306; DOI=10.1016/0378-1119(91)90012-z;
RA   Notarnicola S.M., McIntosh M.A., Wise K.S.;
RT   "A Mycoplasma hyorhinis protein with sequence similarities to nucleotide-
RT   binding enzymes.";
RL   Gene 97:77-85(1991).
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.
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; M34956; AAA25423.1; -; mRNA.
DR   PIR; JQ0894; JQ0894.
DR   AlphaFoldDB; P41508; -.
DR   SMR; P41508; -.
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; 2.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF75553; SSF75553; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   DNA-binding; Nucleotide-binding.
FT   CHAIN           1..979
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000119026"
FT   DOMAIN          419..538
FT                   /note="SMC hinge"
FT   COILED          169..400
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          572..716
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          750..818
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   979 AA;  110566 MW;  30D51C56B56280F4 CRC64;
     MLKLIKIEIE GFKSFADPIS INFDGSVVGI VGPNGSGKSN INDAIRWVLG EQSAKQLRGL
     NMDDVIFAGS KTVKPQEKAM VKLTFKNEDA IEETKQIFTI SRLLKRGQGT NEYFYNDQPV
     RYKDIKNLAV ESGISKSSLA IISQGTISEI AEATPEQRKA VIEEAAGTSK YKLDKEEAQK
     KLIRTNDAID KLQGAIKELE RQVNSLDKQA SKAKIYLEKS KALESVEVGL IVNDLNFFNE
     KLNNLNTSLL EVEQQRNDLE LNIQTYESSI SQTVHFKTEV ESSIQEITSK LDNLKNALSE
     INLQEARIEE RRKLIISGEI VVDQKTKIEE IKKQVESLKI QINASKQREI ELDQQLTRLN
     AKANSLKLQE NDINKEIGVL LEKKSAAAAN INILKQQFEN KSFLSKGIKT IKDNSFLFDG
     YIGLASELFK VESEFSLAIE TVLGAALNQI VMKTSEDVLQ AIDFLKKNLS GKATFIPLTS
     IKEREVREDH LLVLKGQKGF LGVAKELIEF DTQFNKLFGF LLGNILVVDN VDNANRIAKI
     LDHKYTIVSL EGDLFRPGGT ITGGSKLERT SILNYDIKIK EHTNTLKFAE DQIHDLKIKQ
     QTIYNEIETV NSTIQQVKIE ANSINSKLNI LNEELNNLKL NASEIFKEQQ EDQESLNLSF
     DSEKLNIEKQ ISTLTIELNS KKDRLTNLIS EQGKGETKKQ ELDAKLRKLN TQHSDSITEQ
     NRAKFLVEQN QKRLSEHYKL TLEAASEQYS LDLDIEQARH FVDSLKKELK ELGNVNLEAI
     TEFEEVNQRY QEKKQYIEEL TTAKSKIEEA ISDLDKIIIN KTTEIVNLVN NEFNMVFQKM
     FGGGKAEIHF TDKNDILNSG VEISAQPPGK TIKNLRLFSG GEKAIIAISL LFAILKARPI
     PLCILDEVEA ALDESNVIRY VEFLKLLKEN TQFLIITHRS GTMSRVDQLL GVTMQKRGVT
     SIFSVELSKA KEMLKDELK