ID J4K726_9FIRM Unreviewed; 1185 AA.
AC J4K726;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
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:EJP18536.1};
GN ORFNames=HMPREF1140_2461 {ECO:0000313|EMBL:EJP18536.1};
OS Lachnoanaerobaculum sp. ICM7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=936594 {ECO:0000313|EMBL:EJP18536.1, ECO:0000313|Proteomes:UP000006599};
RN [1] {ECO:0000313|EMBL:EJP18536.1, ECO:0000313|Proteomes:UP000006599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICM7 {ECO:0000313|EMBL:EJP18536.1,
RC ECO:0000313|Proteomes:UP000006599};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJP18536.1}.
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DR EMBL; ALJL01000036; EJP18536.1; -; Genomic_DNA.
DR RefSeq; WP_009664049.1; NZ_ALJL01000036.1.
DR AlphaFoldDB; J4K726; -.
DR PATRIC; fig|936594.3.peg.2347; -.
DR Proteomes; UP000006599; 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; 2.
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}.
FT DOMAIN 521..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 227..415
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 444..471
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 671..810
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 850..904
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; 135085 MW; 2A1A47936DBA017C CRC64;
MYLKRIEIQG FKSFANKIVF DFHNGITGIV GPNGSGKSNV SDAVRWVLGE QSAKQLRGGN
MQDVIFAGTE LRKPLGFAYV AITLDNSDHK LDIDFEEVTV SRRLFRSGES EYMINGSACR
LKDISELFFD TGIGKDGYSI IGQGQVDKIL NGKPEERREL FDEAAGITKF KRRKGLALKK
LESERESLVR VNDILTELEK QVGPLERQAK VAKEFLALRE ELKTFDVNSY IMEYDSITQN
LNEYKKREKL LSDDLNDAKA SLERSKQDYE NITADLKKID EELDELRNTR SATSITLQEI
TSHIEILKEQ INSENRNNEN LASRGENIDS DIEKKQKELD KLEEEKNSLQ RLLNEAHEKE
NSVFEELENI DKNINELTKR LEDLKNASEE FNSKNADLRA KKERYKGILE QVRLRKSQMT
QRLLESKTGQ NTLEIKIEEE DKNLSEINAS IDTVNAAKKE LENKNEAIHT EITRFAKVAS
DLQIKYQRES ARLTSMKNIA ERYEGYGNSI KKIMETRDRI GGIHGVVADI IKASQKYEIA
IETALGGRIQ NIVTDSENTA KILIDYIKKN KYGRATFLPL SSVRNSTFSN KEFLKEKGVI
GIASELVEFD SAYVNLVGSL LGKIVVIDNI DNAIAFEKKF RYEYRVVTLD GESLSPGGSI
SGGAFKGAGN LLGRKREIDE LEAEITELLK NYTEANDKVE ALKAERNSIN AKLEENRVQN
QELIIEKNNI AHRRNSLIEK LDELKASSIS VQTDFENIDN ELTEIENETK RLDNTLLNVG
EDFGKVGKDI ESIEKEIQSH RSKRETVVER LNSSKLEYAN ISQRLEFSDE NVNRTKADMD
ALIAEKSGLK GKAEDIIRNI TEKNQRIEEE QRAREELAQK IEELKKKEEE LSEIKETKNK
SQNKIFENRD IYSDRVSLLD RDIYRLRGQI EKSEERISER TNYMWNEYEL TYNSSLELKT
DTGMSLNDIR AKIQELRSKI KALGNVNVNA ISDYNEVSGR YELMKKQHSD ILEAEETLIK
IIEELDIAMK KQFAEKFEEI AKEFDEVFKE LFGGGSGKLV LEEQDDMLEA GIAIISQPPG
KKLQNMMQLS GGEKALTAIA LLFAIQNLKP SPFALLDEIE AALDDSNVDR FAKYLHKLTD
HTQFIVITHR RGTMVSSDRL YGITMQEKGV STLVSVNLIE NELDN
//
