ID A0A084JLB3_9FIRM Unreviewed; 1186 AA.
AC A0A084JLB3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=IO98_13820 {ECO:0000313|EMBL:KEZ89747.1};
OS Lacrimispora celerecrescens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lacrimispora.
OX NCBI_TaxID=29354 {ECO:0000313|EMBL:KEZ89747.1, ECO:0000313|Proteomes:UP000028525};
RN [1] {ECO:0000313|EMBL:KEZ89747.1, ECO:0000313|Proteomes:UP000028525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=152B {ECO:0000313|EMBL:KEZ89747.1,
RC ECO:0000313|Proteomes:UP000028525};
RA Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.;
RT "Draft genome of Clostridium celerecrescens 152B isolated from sediments
RT associated with methane hydrate from Krishna Godavari basin.";
RL Submitted (JUL-2014) 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:KEZ89747.1}.
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DR EMBL; JPME01000015; KEZ89747.1; -; Genomic_DNA.
DR RefSeq; WP_038281872.1; NZ_JPME01000015.1.
DR AlphaFoldDB; A0A084JLB3; -.
DR STRING; 29354.IO98_13820; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000028525; 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; 1.20.1060.20; -; 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:UP000028525}.
FT DOMAIN 521..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 269..296
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 350..380
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 430..485
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 679..881
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 967..994
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; 135946 MW; C9935C4657204908 CRC64;
MYLKSIEIQG FKSFANKIVF EFHNGITGIV GPNGSGKSNV ADAVRWVLGE QKVKQLRSSN
MQDVIFSGTE LRKPQGFAYV AITLDNSDHH LAIDYDQVTV SRRVYRSGES EYMINGSACR
LKDIYELFYD TGIGKEGYSI IGQGQIDKIL SGKPEERREL FDEAAGIVKF KRRKLIAQKK
LDDEKQNLIR VNDILTELEK QVGPLARQSE AAKEYLRLKE DLKKYDVNQF LMETEGIQKQ
MKEIQEKETI VSHDLDDAKQ TSEGIREEYD VLDTYLAELE EAISSARNEN NKSNMETGSL
EGRINVLKEQ INTEQMNAEH IAGRMRAIHA EMQMKMDQAA TYEEERSLIA DQVKAAVKEL
KEAEEVLHSE DEAIRLLEQQ IEEGKSGIID ILNEKASLTA KQQRYETMLE QVNVRRSEVC
QKLLKFKSDE SEQDEQLETL QTEADEIETR IAEGQEAQAF CENRVEELTG EVKRLNKNLN
DKQQEYHTSY TKLESLRNIA ERYEGYGGSI RRVMEVRDRI HGIHGVVADL ITVPKKYEIA
IETALGGSIQ NIVTDSEATA KQLIEYLKKN RYGRATFLPL TSMGNRDSFR QDKALTEPGV
LGLANTLVDT DDRYKGLLNH LLGRVVVVDT IDHAIALAKK YQYSFRIVTL EGELLSVGGS
MTGGAFKNTS NLLGRKREME ELEEICSKAL SDVERLEKEL VMNEGLLGES REELEKIRAE
KQQLYLKQNT VKINIRRIED KKEEIKESYG DLERENGQLE VQIREISASQ QELLTSVDKL
EIQNQDTVGE LERLNGRLET ARTDREQHSK DLSSVQLKTS GLKQKDDFEL ENIRRVKEEI
HRLEEELSGL SNGTNGSNSI IEEKQKEIEV LKGRIEEKKV YSEELEGIIN EKSVQKETSS
KEQKELFRKR EELTGRISLL DKELFRLQSQ KEKLDEWMEN HVNYMWNEYE LTFSTAKDLK
NQEWTSLPEI KRMIQSLKEE IRKLGNVNVN AIEDYKEVSE RYEFMKTQHD DLVAAEGTLL
KIIDELDTGM RKQFEEKFRE IRQEFDKVFK ELFGGGRGTL ELVEDEDILE AGIQIISQPP
GKKLQNMMQL SGGEKALTAI ALLFAIQNLK PSPFCLLDEI EAALDDSNVD RFAKYLHKLT
KYTQFIVITH RRGTMLSADR LYGITMQEKG VSTLVSVNLI EEDLES
//
