ID A0A1V4I6L4_9FIRM Unreviewed; 1186 AA.
AC A0A1V4I6L4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:OPJ55628.1};
GN ORFNames=CLOTH_13870 {ECO:0000313|EMBL:OPJ55628.1};
OS [Clostridium] thermoalcaliphilum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=29349 {ECO:0000313|EMBL:OPJ55628.1, ECO:0000313|Proteomes:UP000190140};
RN [1] {ECO:0000313|EMBL:OPJ55628.1, ECO:0000313|Proteomes:UP000190140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7309 {ECO:0000313|EMBL:OPJ55628.1,
RC ECO:0000313|Proteomes:UP000190140};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium thermoalcaliphilum DSM 7309.";
RL Submitted (MAR-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ55628.1}.
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DR EMBL; MZGW01000004; OPJ55628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4I6L4; -.
DR STRING; 29349.CLOTH_13870; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000190140; 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:UP000190140}.
FT DOMAIN 520..636
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 241..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 733..760
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 810..907
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 990..1031
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; 137810 MW; 76AC504D96D2809D CRC64;
MHLKKIEIRG FKSFPSKTEI IFEQGITSIV GPNGSGKSNV SDAIRWVLGE QSIKSLRGDK
LEDVIFAGSE NKKPMSFCEV ALTIDNKDGI LDIDYSEVTI KRVAYKSGES QFYINNKSCR
LKDIKELLLD TGIGKEGYSI IEQGKIDEIL SGNVSSRRKV FEEAAGISKY RYKKEEGEKN
LKITKENLSR ICDIYDEIEK QLRPLEIQRE KAIKYVDLKK ELKSLEVNSY LKEIEAIDTQ
LKELCSHKEI LQNQLMNLEN KKDKEEKKVY TLEENLNKLD LKINEQNEQL YSLKIEIDHK
KSDLELLNEK IKNIEFNQSK NEKEIVTLKE TMLKNDEYIT NLNKSKQEIS ERLGNLKKEK
NDIDSTIQSY NEDLKNKQKE IERLKDEIIT ILDEKNKKNA KLSSLRTTLD NINEREKTIK
REIEDINQNI KQKHFQLEQY LIKKNEYEER FKNLNKDRNE KHNKSITIKN NLDNIKESIN
TANLKINEYS SKLNIFYEME KQYEGFNKGV KEVLKNKNLK NILGAVAEII NVPKEYETAI
EVALGASLQN IITENEESAK HAIDYLKKNN LGRVTFLPLN IIKGRKINNN EISNVNGVLG
VASDIIKCDN KFKNVVEHLL GRIILTKDID TAISIAKCTN YKYKIVTLDG EVFNAGGSLT
GGSIKSVNNL LSRKRMIEEF EKNIKIENEN LNKFKNYKIQ TELELERIYS DLNDLDIRIK
EEDKLILTNQ SSIYKVNEEI ESLNSLKSKL EREEKGLIQN INYTNELINA TLSEIEDTNK
KSIAIEERVS FINDEKLQKE KLYEKDVAIY NEVNLDIAKL SENLKNIQKD IERMCEEKQS
LENIIKSKEE EIANNKSFKQ DLSEKLILVR VEKEELKEKL NDIELSLKEC KLQRENILSQ
LKDNKENLKH TDEQFIDLKE SIYKLESKLD KLELSQESYF TKLWNDYEIT FYEALKIKDE
FIVIDKKRID NIKREIKNLG NVNVDSIKEY EDIKERYDLY KEQKEDLESS IESIEELIKD
MEQNMKFEFS KNFEKINENF KVVFQKLFGG GHGELRLTDL SNILECDIEI TAQPPGKKLK
NINLLSGGEK ALTAICILFS IILAKPTPFC ILDEIEAPLD DANIYRYGEF LKELSSKTQF
ITITHRRGTM EASNYIYGVS MQEKGISKII SLKIQDAQKF IDEEVI
//
