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Database: UniProt
Entry: R7R841_9FIRM
LinkDB: R7R841_9FIRM
Original site: R7R841_9FIRM 
ID   R7R841_9FIRM            Unreviewed;      1186 AA.
AC   R7R841;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=BN450_02616 {ECO:0000313|EMBL:CDF46218.1};
OS   Roseburia sp. CAG:100.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=1262940 {ECO:0000313|EMBL:CDF46218.1, ECO:0000313|Proteomes:UP000018092};
RN   [1] {ECO:0000313|EMBL:CDF46218.1, ECO:0000313|Proteomes:UP000018092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:100 {ECO:0000313|Proteomes:UP000018092};
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:CDF46218.1}.
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DR   EMBL; CBKV010000259; CDF46218.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7R841; -.
DR   Proteomes; UP000018092; 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   CDD; cd03278; ABC_SMC_barmotin; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 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   NCBIfam; TIGR02168; SMC_prok_B; 1.
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; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018092}.
FT   DOMAIN          521..638
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          167..499
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          672..727
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          752..860
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          995..1032
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   1186 AA;  135451 MW;  1209D42FDDD3A42A CRC64;
     MYLKSIEVQG FKSFANKINF QFHQGITGIV GPNGSGKSNV ADAVRWVLGE QRIKQLRGES
     MQDVIFSGTE LRKPQGFAYV AITFDNADHK LAIDYEEVTV ARRLYRSGES EYSINGTPCR
     LKDVNELFYD TGIGKEGYSI IGQGQIEKIL SGKPEEKREL FDEAAGIVKF KKRKATAQKK
     LEDEKQNLVR VNDILSELEK QVGPLEKQSE KAKIFLKKRE ELKELDVNLF LLENDRMKGQ
     LTDVEEKYAI AKGEYEQAVQ QYDNIKNEYD SIQLRIEELD QEIEIARTSI SDANVTRGKL
     EGEIAVLKEQ IKNAQGNEQH FHDRANTIKE QIQEKEQEKS RLLADKAVYD EEMASLEQSR
     NEAKNSLTQV QQRIEELNTL IEEDKKQIID TLNDRATIKS KMSSFDTMME QLRIRKAELN
     SRLLRAKSDE AERDAEIQSL EEEFRKINDR IIDTNNHLTQ LDEENTAMRA ALTAKDEEIR
     SLQEKYQQSK SKLDTVTNLT ERYEGYGGSI QKVMEQKDRN QGIIGVVADI IKVEKKYETA
     IETALGGNIQ NIVTNDEETA KEMIEFLKKN RYGRATFLPL TSITNPQEFK TPDVLNEKGA
     IGLADSLVQT EKRYSNVAKA MLGRIAVIDT IDHAVKIARK YDYGVRMVTL EGELLVPGGA
     ISGGAFKNNS NLLGRRREME ELEKRVAQSK QAMEAAKAAL EEMRQKRNDL RKSIEEEKAA
     LQELFIKQNT ARMNVVTAQE RKAEAEQGYG DLKSEELEID RKQEQINQDK EAINQELQIS
     QEQEKNLEQA IAQCQKELDG YRAEESGKTS MVGEWDVAYE KLLQKQEFEK ANLSRIESEI
     DRLNRELQEV ELSLSQSQEE ADVRRKSIEE LSATIEASHT TQSDSEVALK EKQTLREELT
     AKQKTFFSTR EELSDRKAGL DKEVYRLNAQ KEKLDDMLDS QINYMWNEYE LTLSSAAELR
     KEDMTDVPAM RKQIAGIKDE LRKLGDVNVN AIEDYKALME RYTFLKNQHD DLIEAEKTLE
     GIIQELDTAM RKQFAEKFEE IRREFDKVFK ELFGGGKGTL ELIEDEDILE AGVRIIAQPP
     GKKLQNMMQL SGGEKSFTAI ALLFAIQSLK PSPFCLLDEI EAALDEGNVS RFAKYLNKLT
     KSTQFIVITH RRGTMEQADR LYGITMQEKG VSTLVSVNLI DSSLEN
//
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