ID D9SLC7_CLOC7 Unreviewed; 1191 AA.
AC D9SLC7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Clocel_1899 {ECO:0000313|EMBL:ADL51643.1};
OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL51643.1, ECO:0000313|Proteomes:UP000002730};
RN [1] {ECO:0000313|EMBL:ADL51643.1, ECO:0000313|Proteomes:UP000002730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC {ECO:0000313|Proteomes:UP000002730};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Clostridium cellulovorans 743B.";
RL Submitted (AUG-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}.
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DR EMBL; CP002160; ADL51643.1; -; Genomic_DNA.
DR RefSeq; WP_010077140.1; NC_014393.1.
DR AlphaFoldDB; D9SLC7; -.
DR STRING; 573061.Clocel_1899; -.
DR KEGG; ccb:Clocel_1899; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000002730; Chromosome.
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; 2.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000002730}.
FT DOMAIN 526..643
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 231..310
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 346..380
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 437..516
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 682..782
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1000..1041
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 1191 AA; 135539 MW; FBC23EBABA5C051F CRC64;
MYLKAIELRG FKSFADKTEI ELKDGITAIV GPNGSGKSNI SDAIRWVLGE QSVKNLRGGK
MEDVIFAGTA YRKPVGLAQV ALILDNSDHG LPLDYSQVTI SRRLFRSGDS EYYINNTKCR
LKDIHELFMD TGIGKEGYSI ISQGKIEALL SGSSDERREL LEEAAGIVKY KSRKNESEKK
LNLTEQNIVR LNDILSTYEE RLGPLEIESE KAKEFLKLSE SLKNNEISLM IDSVEKIQSK
LEVNKEALKQ QEEALKEIYE DKSKLKDEQN KLIELQEELE KEVFKEREEF QKQNESREEV
RAENILLEER ISNSNVIAEK EVVEVENLRK KITDMQAIST QHSLDIKATD EKLKELTSAI
ENTEQEVQSV NDSISIQEVN IDKAKVEASD LDVKIFDFTS EIAVINNEIE NVKLKNQGIL
ASMESNENTI AINTNTKLAL LKETEELKKK SLELEDQSFE SKKNLSRLSR NLTIEEKDLK
ELTNEKTKGE TNLSFLNKLE EQYEGYTKSV KNLMSHIKEN RIDNLQGEVN VLGEVISVNR
KYETAIEIAV GSGISNIISS TEKDAKKLIM HLKNNNLGRA TFLPLDTIRS NVISVDKNIA
NMKGYLGIAS ELIEYEARFK KAIDFVFGRT LIAEELDAAT AIAKASNYSY RIVTLQGEVV
SPGGSLSGGS LYSKSLNIIG RKREIEDISD KLKEISDKLE DKKIKIENLR KEIALSDEEI
LNLTDKIHFN NIEKTKVEER VSALEKEILN VKKVVSTNRE IVSKLKTELE EKQSLLNDKN
ESVLRFKNRK EQLKVFIEEE ESKKQQVSKS ISERKDMLTS YKIEEAKTIE ALSSKKSSFE
SLKYEIEEIS ERIKTKENEI ILSKSAIEAM KEKIKNNNNI LESINSYIIS KNKFFEEIEG
KKLGFRERQK KVNDQLEIIN DTINSREELK HRQEVAIAKS ETEYENILNK LNEEFNLTLA
EAYEYKVENL EVASVKDIIY SLKRQISSLG VVNVGAIEEY KEIKEKYTFM NNQREDLINA
KDELMKVIEE MTEKMKEVFN ENFEKLKVLF NETFQQLFKG GSGDLLINGD DVLLSPIEIN
VQPPGKKLQN INLMSGGEKG LSAIALLFAI LKMKPTPFCI LDEIEAALDD VNVSRYAEFL
KKFSSNTQFI VITHRKGTME ASDVLYGVTM EEKGVSKIVS VDLTNNNMEA V
//
