ID F0Z4P7_9CLOT Unreviewed; 1186 AA.
AC F0Z4P7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=HMPREF0240_04100 {ECO:0000313|EMBL:EGB91063.1};
OS Clostridium sp. D5.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=556261 {ECO:0000313|EMBL:EGB91063.1, ECO:0000313|Proteomes:UP000003978};
RN [1] {ECO:0000313|EMBL:EGB91063.1, ECO:0000313|Proteomes:UP000003978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D5 {ECO:0000313|EMBL:EGB91063.1,
RC ECO:0000313|Proteomes:UP000003978};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., White A.P., Crowley S., Surette M.G., Strauss J.C.,
RA Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium sp. D5.";
RL Submitted (MAR-2010) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL870820; EGB91063.1; -; Genomic_DNA.
DR RefSeq; WP_009005373.1; NZ_GL870820.1.
DR AlphaFoldDB; F0Z4P7; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000003978; 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; 1.10.287.1490; -; 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.
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:UP000003978}.
FT DOMAIN 521..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 234..317
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 374..401
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 430..485
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 679..706
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 735..916
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; 135806 MW; 67E041F76A6443B0 CRC64;
MYLKSIEVQG FKSFANKIKF EFHNGITGIV GPNGSGKSNV ADAVRWVLGE QRVKQLRGGT
MQDVIFSGTE NRKPLSYASV AITLDNSDHQ LPVEYEEVTV TRKLYRSGES EYLINGAGCR
LKDINEMFYD TGIGKEGYSI IGQGQIDKIL SGKPEERREL FDEAAGIVKF KRRKNLSVRK
LDEERQNLTR VNDILSELEK QIGPLKRQSE VAREYLKKKE ELKTYDINMF LLETERIKEQ
IRELDSKYQI ASDELEEASV RYEDMKTEYE AIEEEVDSID FSIEKAKSQL NETTLLKQQL
EGQINVLKEQ INTVRMNDEH YDNRLGTIRV EIETRQAQRA ELAKEQTSVR ARLQEVAKSD
AGAKEELIDV QSRIASGTAQ IEQSKAEIME LLNNRASTKA KIQHYATTQE QITTRKSELG
RMILEVSSEA EKQNDILSSY ENELQQISGK IAAYTEQISS NEQEIEKLQQ ELSGKQEQLR
IGQTAYHRES SRLESLKNIT ERYDGYGNSI RRVMSNKDRE KGLIGVVADI IKVEKEYEIA
VETALGGNIQ NIVTDNEETA KRMIAYLKQN KFGRATFLPL TSMHGGGGIR QQEALKEPGV
IGLASTLVQV EDRFQGLAEQ LLGRTIVVDN IDNGIRLARK YKQSLRLVTL EGELMNPGGS
MTGGAFKNSS NLLSRRREIE EFEKTVGMLK KEMDDCEQSV NEIKAKRAAC YSTIDEIQQK
LRKASVIENT AKMNVEQVQN RQREAKLRCE GYLKEQEGLE LRLQEILDNE DSIQMELETS
EALEKELNAR IEELQKSLES DREKETIQLR HSEEVHLSYA SLEQQNAFIL ENITRIQEET
EKFEIELKEL DINKGNASEE IQEKEEKIRD LRETIENSKE LFAEIDAEIK SQVAKREELN
QKHKEFLGKR EELSKHMSEL DKECFRLSSR RESYEEASEK QINYMWDEYE LTYNHAMELR
NENLTDLSYM KRQIQALKGE IKKLGSVNVN AIDDYKSVSE RYEFLKGQHD DLVEAEATLM
KIIDELDAAM RKQFEEQFAL ISKEFDIVFK QLFGGGKGTL ELMEDEDILE AGIRIIAQPP
GKKLQNMMQL SGGEKALTAI SLLFAIQNLK PSPFCLLDEI EAALDDNNVV RFAQYLHKLT
KNTQFIVITH RRGTMTSADR LYGITMQEKG VSTLVSVDLL EDELDK
//
