ID A6LSM4_CLOB8 Unreviewed; 1185 AA.
AC A6LSM4;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Cbei_1172 {ECO:0000313|EMBL:ABR33354.1};
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR33354.1, ECO:0000313|Proteomes:UP000000565};
RN [1] {ECO:0000313|EMBL:ABR33354.1, ECO:0000313|Proteomes:UP000000565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR33354.1, ECO:0000313|Proteomes:UP000000565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX PubMed=21962126; DOI=10.1186/1471-2164-12-479;
RA Wang Y., Li X., Mao Y., Blaschek H.P.;
RT "Single-nucleotide resolution analysis of the transcriptome structure of
RT Clostridium beijerinckii NCIMB 8052 using RNA-Seq.";
RL BMC Genomics 12:479-479(2011).
RN [3] {ECO:0000313|EMBL:ABR33354.1, ECO:0000313|Proteomes:UP000000565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX PubMed=22433311; DOI=10.1186/1471-2164-13-102;
RA Wang Y., Li X., Mao Y., Blaschek H.P.;
RT "Genome-wide dynamic transcriptional profiling in clostridium beijerinckii
RT NCIMB 8052 using single-nucleotide resolution RNA-Seq.";
RL BMC Genomics 13:102-102(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}.
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; CP000721; ABR33354.1; -; Genomic_DNA.
DR RefSeq; WP_011968510.1; NC_009617.1.
DR AlphaFoldDB; A6LSM4; -.
DR KEGG; cbe:Cbei_1172; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR Proteomes; UP000000565; 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; 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}.
FT DOMAIN 525..642
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..194
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 234..380
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 437..516
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 681..788
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 817..907
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 999..1040
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 1185 AA; 135935 MW; FC0B35856D88A7F6 CRC64;
MFLKSLEIRG FKSFADKTEL KFKQGVTAVV GPNGSGKSNI SDAVRWVLGE QSVKVLRGGK
MEDVIFAGTQ FRKPVGLAQV SLTLDNSDEK LATEYNEVVV SRRIFRSGES EYLINNSKCR
LKDVINLFMD TGIGKEGYSL IGQGKIEAIL SGKPEDRRNL LEEAAGIVKF KNRKEEAEKK
LSNTDENLVR INDILSTYEE RIEPLRIERE KALEFTDLSN NLKKKEVSLI VHTIDKMEEE
LKGFNEDLNL KIKEIEDKRK EVSSYKSQLK ELEMKIEKLE KKNLEEKEKY YSLKETVSED
EKSIELYKER IKSFEEKINR NNYELDDILI KVNQLNENKK LLESELSERL KEQRLREEDI
VNLEENNIKS SKELKSIDEE IKSLREGEFE LLRSNSDMKN EITMLNKDLS LREEKKETLN
SSISFLENNI VINLATYKDL TNESEKNKDN IKLLNMQIVE HKKKIGSLSA NLTKKENELR
ELSGTLTKLD ANRSMLENLE KHYEGYNRSV KSLMESIHRE RITAANDTKV LGEIFTVGKK
YEVAIEIALG AAISNVITKN EEIAKVLIGY LKKNSLGRAT FLPLNIIKGK KLELDRSITE
ANGYIGIASD IISYDKEYKN IMDYSLGRTI ICSDMDCALN IARIGKYNYR IVTLDGEIIN
PGGALTGGSI KGKNSNVLGR KREIEELVLD ISNKKEKYEE LKILVQDIKK EIQDLDEDML
NKRDEVHEKN IELTKKESEI KGLQSDTDKL KRNLETAKEE IKRIAGEREA ILEKIRAKES
EVQVIESENT ANKSKSIELE QLMKIKVQEV NDSDTKLTEM KISKAKLDEA IENKKNEFLR
IEKEIKDLEI KNELLNNENE ENKKNIESLN LDIKAKNKNI EENNINISNL EVNFKDDEIL
KEKLKQEFKE KDNVISGILD EVSLKEMEVN KREVIKAKKE NDREHVYKKL NEELELTYAE
ALDKCEPVVD EEALKQEIFV TKGKITKLGV VNLAAIEEYE EIKEKYEFMS TQAEDLENAK
RELNAVIEEM TNEMKSLFKE NFKILNYNFD KTFKDLFKGG SAELILGEGD ELTANIDINV
EPPGKKLQNI NLMSGGEKVL SAIALLFAIL KMKPTPFCIL DEIEAALDDA NVYRYAEFLK
MFSKNTQFII ITHRKGTMEV SDIIYGVTME EKGVSKVVSV DFSDS
//
