ID H2JJL0_9CLOT Unreviewed; 1190 AA.
AC H2JJL0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=Clo1100_1774 {ECO:0000313|EMBL:AEY65984.1};
OS Clostridium sp. BNL1100.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=755731 {ECO:0000313|EMBL:AEY65984.1, ECO:0000313|Proteomes:UP000007324};
RN [1] {ECO:0000313|EMBL:AEY65984.1, ECO:0000313|Proteomes:UP000007324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNL1100 {ECO:0000313|EMBL:AEY65984.1,
RC ECO:0000313|Proteomes:UP000007324};
RX PubMed=23209234; DOI=10.1128/JB.01908-12;
RA Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a Cellulolytic
RT Mesophile Isolated from Corn Stover.";
RL J. Bacteriol. 194:6982-6983(2012).
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; CP003259; AEY65984.1; -; Genomic_DNA.
DR RefSeq; WP_014313357.1; NC_016791.1.
DR AlphaFoldDB; H2JJL0; -.
DR STRING; 755731.Clo1100_1774; -.
DR KEGG; clb:Clo1100_1774; -.
DR PATRIC; fig|755731.4.peg.1760; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000007324; 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; 2.
DR Gene3D; 1.10.287.1490; -; 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; 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}.
FT DOMAIN 525..644
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..380
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 444..478
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 777..804
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 833..986
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 1190 AA; 136447 MW; 3615114199AB4F9D CRC64;
MYLRKLEIQG FKSFADKISL DFNSGITAVV GPNGSGKSNI GDAVRWVLGE QSAKTLRGSK
MEDVIFAGTE HRKPVGFAEV SLTIDNDDNY LPVSYSEVTI TRRVYRSGES EYYINKTSCR
LKDIHELFLD TGIGRDGYSI IGQGRVDEIL STKSEDRRLI FEEASGIMKY KVRKQDAERK
LDLTEQNLVR ITDIINELES QLEPLREQSE AAKKYLTLRE SLKELEVNVY LNNIDKLKEK
IKEYENQFKD IRDNIEAEER RLRSITTQNQ QKTELLKNLD EQITEARGKF YIIEANLEKN
SSEVKLKNEK INSLDGNIVR LNEETSEISS KLELLNTEEK NRQKKIEYLN GQYNDFSKKL
EKYQSELDGI LSTLDESERH IEMLKSGIMD KLDIQSDKRT QINNIKNHIE NMRKRQNSIG
TEIYSLKLEK DKDNMKKEDL IESIRNTSTL IKHSSEKINE LNNEKTELKG TLSELEKQHG
IIRTDIQVKT SRHKMLKDME NSMEGYSRSV KEVMTACKQS PDLGKGIHGT IAQLVEVDKK
YETAIEMTLG SALQNIVTSS EDAAKKAIEF LKRNRVGRAT FLPITSVKGK RLDDNTLRRL
ENCQGFCGVA SDLVTSDPAY NGIVLNLLGR VVVTENLDSG ISIARKFGYT FRIVTLEGDI
LSTSGSMSGG SSDHRSSGIL SRSREISELE NIIEGLKKDE IKYGVKINDV RQMLLEIDTE
FNEHNNKLRD NELIKTRDEN HLQMIEDNLK KTDAKIGMLI NEKDQMAKQE QETLLEQQKY
EAELEAIETD ISETKSIIAE HQEKFKADQT VRDDLHQEIT DFKISVNSIT ESIQSVTENL
DRIKGEREAL TRSHTRKQEE INKANTEIEL LKQEINGLDN STRKLQDEKT GKTLEIDRLV
EEKKVLEEES TDFIEKLNAT NKTIHLLHEE YNRIDIKKAK AEAEMKSIQD RMWDEYELTY
SNAVELKKEI ENISEAQRNI SEYRAQIKAL GPVNVSSIDE YIKTKERFEF MSVQKNDMEQ
AKDKLHKIIY EMVQVMKKQF VEQFKLINEN FGIVYKELFG GGRAELIISD EDNVLESGIE
IEVQPPGKKL QNMMLLSGGE RAFTAIALLF AILRLKPTPF CLLDEIEAAL DDANVYRFGE
YLKKYSQNTQ FIMVTHRKGT MESADTMYGV TMQEHGVSKV VSMKMGEMAS
//
