ID E4Q6W2_CALOW Unreviewed; 1177 AA.
AC E4Q6W2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, 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=Calow_0981 {ECO:0000313|EMBL:ADQ04545.1};
OS Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632518 {ECO:0000313|EMBL:ADQ04545.1, ECO:0000313|Proteomes:UP000006889};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OL;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor owensensis OL.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ04545.1, ECO:0000313|Proteomes:UP000006889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700167 / DSM 13100 / OL
RC {ECO:0000313|Proteomes:UP000006889};
RX PubMed=21216991; DOI=10.1128/JB.01515-10;
RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL J. Bacteriol. 193:1483-1484(2011).
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; CP002216; ADQ04545.1; -; Genomic_DNA.
DR RefSeq; WP_013411934.1; NC_014657.1.
DR AlphaFoldDB; E4Q6W2; -.
DR STRING; 632518.Calow_0981; -.
DR KEGG; cow:Calow_0981; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000006889; 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 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:UP000006889}.
FT DOMAIN 522..636
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 241..401
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 444..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 677..928
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 989..1026
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 1177 AA; 137073 MW; E0B62DA1A9AB2EC5 CRC64;
MYIKWLEIYG FKSFCEKTRI EFQKGITAIV GPNGCGKSNI TDAIRWALGE QSLKILRAAK
QEDLIFAGTE KRKSQGFAEV SICFDNSNGV LPIDYQEVVV TRRLFRSGES EFFINKIPCR
LKDVYELFLD SGLGKDGYSI ISQGRVDEII NARPVDRYRI FEEACGITKY KYRKEETERK
LKTTEENIQR LQDVMFELST QLEEIKPDVQ KAKTYLQINQ KLQSLKKEKY VYEYNLTGRR
YNDLLLKEKQ LNEELERLIH LRRELEKSIN QSESQIDLLT QHIEKTKLSY NDIKSELIEA
TTQLKFLKKQ QENKQQLKED LSSQILQLER QKEELKKSIE ELQKGISEKE EEHRSILEVH
TKLQKQITAL KENITEVEAE IQKKETELIE CISQIEKFNQ KLNGILHLST TLENRKEKIV
EQTNAILSEL EKLTIAQNTK KSKLVELDNE RKKLVILVED LNQQVSEKER HLTNLKNLVD
DISKQLIKKQ EKLSILKMME ESYEGYSKTI KEIFKRVKNL PICLYGTVGS LISVKREYLK
AIETALSSSL QHLVVKNEDD AKRIIEMAKN EKLGKVTIIP VNTVAVLSQK EDINADGFLG
FADEFVEIND ELRKVVEFLL GRTLVFDTID RAIEYQKKVG YKARCVTLSG ELISPGGVFV
GGEKKADFSL LERKVEKEEL EVDVKNLSSR LEEMDKLIIE SSKVLYKLKT AKQEGEKSLN
DLLSKMSELE REIEMYDYKI KQLIQNKDAL ENEKNLIYEQ LITLECDIKS SQERLENLKK
SKEGFEKEIS NLKTALSKLK EDYNFLDSKF TKAIEEKNKI EAELSILKHK LESKSYNMIE
IENQKTYRFN EKVKCEENIR ELEEQIFQTS KEIEEKKQKA EEFKNNLQQL EKDYFELSER
YNSEQKRLHE ASDKIQEIEK KIGQIALEKH DLENYMKNIK EKYFETFNEE IHTSNKEVFW
SKEKEDELER CTAALSELGE VKLYSIDQEK RLQERMQFLQ KQIEDLQKTT DELKRLISHL
EKNMKEIFLE NFEKIKSLFS EIFFELFGGG SCDLKLIGQD GELGVDIDVK PPGKKLQNIN
LLSGGEKALV AIALLFAFLT FKGSLLCILD EIDSSLDEVN VQRFAQYIKN LNSQSQIIIV
THRKPTMEIA NTLYGVTMEE RGVSKVLSLN IEKIQKG
//
