ID R7P8B3_9CLOT Unreviewed; 976 AA.
AC R7P8B3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=BN733_00750 {ECO:0000313|EMBL:CDF20582.1};
OS Clostridium sp. CAG:609.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262827 {ECO:0000313|EMBL:CDF20582.1, ECO:0000313|Proteomes:UP000018389};
RN [1] {ECO:0000313|EMBL:CDF20582.1, ECO:0000313|Proteomes:UP000018389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:609 {ECO:0000313|Proteomes:UP000018389};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDF20582.1}.
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DR EMBL; CBKL010000032; CDF20582.1; -; Genomic_DNA.
DR AlphaFoldDB; R7P8B3; -.
DR STRING; 1262827.BN733_00750; -.
DR Proteomes; UP000018389; Unassembled WGS sequence.
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:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 6.10.140.1720; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 3.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}.
FT DOMAIN 420..538
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 168..202
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 235..406
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 569..705
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 976 AA; 110377 MW; A7D3575F43D80ED3 CRC64;
MYLKSIRAQG FKSFADKLDL EINPGITGIV GPNGSGKSNI VDAVRWVLGE QSVKSLRGQN
NMTDCIFSGS ESREAQKRAM VALVFDNKDH YLHSDFNEVE IKRIVYATGE NEYYINNARV
RLKDFTDLFI DSGAGVNAFN IISQGNVTDI VNSKSSDRRI IFESAAGVLK YKKRKEESLK
KLEKTEENLT RIKLIIDELS KTVEPLKEQS IVAKKYLSIK GELESIDIAL IAKDITDLNL
EYSKITEEIK SLKEKLVTLK DDGKSVELEK LKLKNIELED AVNKKREELL KITEQISDLN
GEKKLTIERQ KYESNQTIID NNLMKLKEQE LSLNKNITIL TREVEDIEKS IADERKKGED
VKNELLVLKV KKSTSTNALL EQNKKKFLLE NKIEILENNI LSAESAPQSV RNILNNPRLY
GIHNTIGKLI DIPDNYMIAT DIALGAASNY LVVENENSAI NAIDFLKERK LGRATFFPLN
VIKGRLASSE IINDIKNING YIGILSDLVN YDAKYKNIIE NQLGQVILVD NERTLNIVGK
LINYKYKVVS LDGEILHIGG SITGGTSKKN TMLNEKNELN KLKSDLQKLE INIKDLSSEV
TSLNDKEEEL TERETVLNKY VILLNDELFN KKTNLSRVTE EYKNVTSELE GINDLKSNKL
DEHLIELMNE INKLSENKEL IEKDIKSITK EKNNLNDEIA IIDHELRDSN NSYNAINSEL
KNKEVSSGKL EVKLDNLLDS LNNEYNLTYE AAQVKYNLEM DPDIARSHCQ NLKKELNSLG
NVNTGSIDEY ERLSKRYEFL TSQKFDLESA STELKGIINE MDDIMVEKFA KSFESIKKEF
SKIFKMMFKG GKGELQLSNP DDLLNTGIDI IAIPPGKKIN SPVSLSGGEK ALTAICLLFA
MLEVKPSPFV ILDEAEAALD EVNVDMFGKY LSEEKSRSQF IVITHKKRMM EYADSLYGIT
MQESGVSKIV SAKLEN
//