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Database: UniProt
Entry: R6PB61_9FIRM
LinkDB: R6PB61_9FIRM
Original site: R6PB61_9FIRM 
ID   R6PB61_9FIRM            Unreviewed;      1193 AA.
AC   R6PB61;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=BN582_00981 {ECO:0000313|EMBL:CDC20750.1};
OS   Eubacterium sp. CAG:274.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262888 {ECO:0000313|EMBL:CDC20750.1, ECO:0000313|Proteomes:UP000017904};
RN   [1] {ECO:0000313|EMBL:CDC20750.1, ECO:0000313|Proteomes:UP000017904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:274 {ECO:0000313|Proteomes:UP000017904};
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:CDC20750.1}.
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DR   EMBL; CBEX010000085; CDC20750.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6PB61; -.
DR   STRING; 1262888.BN582_00981; -.
DR   Proteomes; UP000017904; 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; 2.
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   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; 2.
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:UP000017904}.
FT   DOMAIN          525..642
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          227..254
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          290..457
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          684..718
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          761..984
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   1193 AA;  136686 MW;  F10BABBD70776F36 CRC64;
     MYLKSLELQG FKSFPEKIKL DFNKGITAVV GPNGSGKSNI ADAVRWVLGE KSAKSLRGNK
     MEDIIFNGTE NRKPLSFAEV SMIMDNSDKK LNLDYPEVTV TRRVYRSGES DYLLNGTKCR
     AKDILELFMD TGVGKEGYSI IGQGRIDEIL SNKSEDRRML FEEAAGIVKY RTRSFEASNK
     LAKERENLVR VNDIIATLET QVGPLEVQAE KAKKFISLSN KLKTVEVNRF VIEADRFEND
     IKEVEKSISQ LGNDVLRERR QEEVLQKKRT SLKDDLSNVD LQYEENSNSI GEKRSQVEQK
     ENDIKMCESE IQHFNENIER LNKSIDQNKK AIEDKNNESD ALDAKIVAKT LEAERKKKSY
     EEKKSAYTDL ETKVTESEEL FNRFNSDIRD KMNRSADISS EISKINAKLS QLKDRKNTVS
     EDISVLNGQL KEKEIALAVE EQKITRIDNE IEKISNNIEN DNVTLSELSG KINETKKKQL
     DMTKSIQDKQ SRLRILSELE NSYEGYYGGV KAVLSQRDKK ISGFEGICGA VGELITLDKK
     YETAIEIALG GAVQNIVAKN ENDVKKAISY LKTNNKGRAT FLPMTAIKPK TINNKTDILK
     NTGVIGIAKE LISYDVQYEN IMSSLLERVI IVDTIDNGIA LSKKTNYSYK VVTLDGELFN
     VGGSMTGGSI SKRSTGIFSR GREIGELREN LKVLVSEYNE LNSELDSMNN SITESNDNLK
     KSNEMLQSLH INRARSVAEV TKSKEYVDDY KKRIEYSDVE SEKLESTILE DEKQVKQYEN
     DLEAITDEIN SVNEKIQEYQ SKIQENRDIR ESSIREINDL KLDINQINNE IYNFNYNKKR
     IETEVMELNT GIENFKSEIL DYENQIANKE KNKQSIFENT EQLKEEYSKF IKMQEELINY
     KNEVNKNLDE LEKSIQRQTE TKNAIEKQLS RFEIKKEQLE NERKNLYNNM WEEYEITYVV
     AKNYERLDMS SEDLVKEERN LKNQMKALGN VNMNAVEEYA EVSEKYQFLI KNRDDIKQSE
     EKLIGIIEQL NVLMEEQFRE QFKVISDNFA ETFKEMFGGG EASLKLSNDQ DILNCGIDII
     VQPPGKTLQN MMLLSGGEKA LTAISLLFAI LKMKPSPFCI LDEIEAALDD ANVNRYADYL
     KNFVDDTQFI VITHRKGTME AADILYGVTM QEKGISKLVS VKFDENYNLD KEA
//
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