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Database: UniProt
Entry: R7L5T7_9FIRM
LinkDB: R7L5T7_9FIRM
Original site: R7L5T7_9FIRM 
ID   R7L5T7_9FIRM            Unreviewed;      1187 AA.
AC   R7L5T7;
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=BN622_00481 {ECO:0000313|EMBL:CDE82587.1};
OS   Ruminococcus sp. CAG:353.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262955 {ECO:0000313|EMBL:CDE82587.1, ECO:0000313|Proteomes:UP000017936};
RN   [1] {ECO:0000313|EMBL:CDE82587.1, ECO:0000313|Proteomes:UP000017936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:353 {ECO:0000313|Proteomes:UP000017936};
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:CDE82587.1}.
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DR   EMBL; CBJQ010000228; CDE82587.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7L5T7; -.
DR   Proteomes; UP000017936; 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; 1.10.287.1490; -; 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.
DR   SUPFAM; SSF57997; Tropomyosin; 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:UP000017936}.
FT   DOMAIN          523..639
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          167..201
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          227..275
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          304..366
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          402..429
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          458..492
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          680..840
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   1187 AA;  132788 MW;  3610810457CAF353 CRC64;
     MYLKSLELQG FKSFPDKVKL DFGKGITAVV GPNGSGKSNI GDAVRWVLGE QSSKTLRGAK
     MEDVIFAGTQ LRKPVGFASV TLNIVNDKGL LNIDAPEVSV TRKLYRSGES EYIINGSQVR
     LKDVTELFMD TGLGKDGYSI IGQGRVAEIV SSKSNERRDI FEEAAGISKF RYKKAEAQRR
     LTQAEDNILR LTDIISELES RVEPLRKQSE KAAQFIELSD EKKSLEITVW MHELDELRTR
     LNELGEKVLI NATEYNNTET DIDRLEEEYR IVYKDIAAGN IRIENLNNAV LEEERSNTAI
     HSDIAVFKND IEHCRKAIED LEKQMESAKL SDSENRRLTE EKLEEIKRIE ADILTTDREY
     SDAEREFAEA VGQQDGFEKE FSGHSEQLNK MYIRQSELNI TVNTSDNMIK EAEEQKQAAE
     KQLETIVSGA QNLDSERKEV TDGLALLAEK RDEQTNRISG LNRLYASKTE KLKAAEKEQN
     DLTMSVREKE QKMRLLRDLE NSMEGFGHAV KQVLSAGKNG RIRGIIGSVA QIISVPSEYS
     LAVETALGGA LQNIVTENED AAKRGIGLLK ETKGGRATFL PITSVKGNRL NESGLDGCVG
     FVALGCDIVT YDPKFTGIVN SLLGRTVIAE DIDCAGNIAK KYGYRFRIVT LDGQVVNAGG
     SFTGGSANRS AGILTRKNEI EKLNGEVTDL TGKLDELKSR TASLRAETDK MRIDIEAAND
     DLRAMDQDKI RFESELKRIE QVAEQSVNGR KNAEETIARF EKRLSDIRAA AEKAGAELAR
     LCQEISAAEE KSGEDKRIMD ELKSRRDSLS SKMSDMKIKK TALEKDLEAV KESIKALEEQ
     SRSIGDSSVR SAMAIEEQNR IIAEKNELIA KREKALESSG SRTEDIHRQI SLTQAENLEK
     ERQSVEIRQK IKVLTDDKEK LGAEKTRLEE RRKTSQSAYD KIVSDMAEQY ELYPSEAASL
     IIPDADKGEI TARLNTIKQK IRNLGTVNLS AIEEYKEVSE RYEFMSGQLS DINSSKRELE
     KLIDELTETM KTRFAESFKE INANFKRIFT ELFGGGRAEL VLTDPDEVLE SGIEINVAPP
     GKVIKNLSLL SGGEQAFVAI AIYFAILKIK PAPFCILDEI EAALDDVNVS KYAHYLRNFT
     DTTQFITVTH RRGTMEEADV MYGVTMQEKG ISRLLKMEQP PADIEAE
//
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