ID I7LBM3_9LACO Unreviewed; 1186 AA.
AC I7LBM3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=BN53_06445 {ECO:0000313|EMBL:CCI85721.1};
OS Lactobacillus pasteurii DSM 23907 = CRBIP 24.76.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423790 {ECO:0000313|EMBL:CCI85721.1, ECO:0000313|Proteomes:UP000009311};
RN [1] {ECO:0000313|EMBL:CCI85721.1, ECO:0000313|Proteomes:UP000009311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRBIP 24.76T {ECO:0000313|Proteomes:UP000009311};
RA Cousin S., Bouchier C., Loux V., Ma L., Creno S., Bizet C., Clermont D.;
RT "Draft Genome Sequence of Lactobacillus pasteurii CRBIP 24.76T.";
RL Submitted (JUN-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:CCI85721.1}.
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DR EMBL; CAKD01000023; CCI85721.1; -; Genomic_DNA.
DR RefSeq; WP_009560275.1; NZ_CAKD01000023.1.
DR AlphaFoldDB; I7LBM3; -.
DR STRING; 1423790.BN53_06445; -.
DR PATRIC; fig|1423790.3.peg.115; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000009311; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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 Cell cycle {ECO:0000313|EMBL:CCI85721.1};
KW Cell division {ECO:0000313|EMBL:CCI85721.1};
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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000009311}.
FT DOMAIN 515..635
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 269..451
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 683..899
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1004..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; 134751 MW; 421D83727DDB1D4C CRC64;
MPLTELIIDG FKSFADKTTI HFNQGITGIV GPNGSGKSNI TEALRWVMGE SRIKSLRGDN
MKDVIFAGSQ FRKPMNRAEV TLIFDNRDRQ LKFDSDQVAV TRRLLRSGDS EYLINKQQVR
QKDVRELFLD SGLSQNSLAI ISQGRVDQIL NSKPEDRRFI FEEAAGVLHF KNQKESAANQ
LAKTSDNLIR INDIVKELEK QLEPLHEESS LAKEYLFQKN KLDHDLKILL ALEIEDLAGQ
KSTLKDKADK NQLVLNKLDA EVKQSQTAVS QKRDLYESLR QKSEDLQKQL LEISNKLSDL
NTELQISNQS KQFDQATQNE YQKQIVDLQA QLKQLHLELE TFVSDEQKFE AQRKQLQDQR
LEILGKLEDD PESLNQKLED ERNNYIQLLQ DQTSNNNELV YLKTELKRAQ EDRSYKGDDV
SGQLEKAKAE LAKLEEQGSK LKTQRQKTNS ELTNIASRLQ KKQADSSNLK SLVNNQRGKL
QQLTARQEAL VNIQKRHEGY YYGVRNILNH LEEYPGVIGV VGELLSFPNE YEAAMTTALG
SSVQNLVTDN RESARDAINR LKQNHAGRAT FLPLDALRQY EIPASTITSL QSFEGFIGIA
SDLVTSRDAD ISVAINYLLA NVIIVDKIET AMAVSSRINR YRIVTLDGDV ISPGGSMTGG
MRNERSNSPL QTMAEISKLT ELIENAKKQL EIDNTSLADL ELELEKLASK HAQLNKQLLE
QNQAINSLAI SYQSQDKEVK RLSDLVKLYN NELQERQAEI DKLLVKQEKL TKQQVEFERL
TQVQKDKISQ IQLRIKDFTA LNQKLQLEVG KIDPQIAVYD NKLENINKQK RDKQKQVQAL
DQQLTKLKEK FANLTKESQL SGKRQAEIQV ELKSMQIAKT QLEEQLADLS SELGQTNAQI
NSLDQVASRN YELRKDVAIE QEEYSVKLAK INSQMMQKLD LLSQEYSLTY EAAKAEVELE
NTPENRADLH RRVKLCKMSI EEIGPVNLKA IDDYKNIKSR YEFLSQQQSD LLSARKNLEE
SMKKLDQEVE KRFMDTFNNV ADSFSQIFPI VFGGGSAKLL LTEPDNPLET GIEIIAEPPG
KKLQRLSLLS GGERALTAIT LLFAMIQISP VPFCVLDEVE AALDDANVTR FGKFLKRYDL
KTQFIVITHR HGTMEEASQL FGVVMQESGV SQVLSVSLKD LKDEVE
//
