ID Q1G9K8_LACDA Unreviewed; 1181 AA.
AC Q1G9K8;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
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:CAI98180.1};
GN OrderedLocusNames=Ldb1379 {ECO:0000313|EMBL:CAI98180.1};
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI98180.1, ECO:0000313|Proteomes:UP000001259};
RN [1] {ECO:0000313|EMBL:CAI98180.1, ECO:0000313|Proteomes:UP000001259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14
RC {ECO:0000313|Proteomes:UP000001259};
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; CR954253; CAI98180.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1G9K8; -.
DR STRING; 390333.Ldb1379; -.
DR KEGG; ldb:Ldb1379; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR Proteomes; UP000001259; 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 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:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000001259}.
FT DOMAIN 510..631
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 162..196
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 229..270
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 313..340
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 405..478
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 672..853
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1181 AA; 132657 MW; 2D5334E06C1CC281 CRC64;
MILEGFKSFA DKTVIDFTKG ITGIVGPNGS GKSNITEAIR WVMGEGSAKS LRGRNMKDVI
FAGSQFRKPL NRAEVTMVFD NRDRELDFSA DQVSITRRIL KSGDNEYLIN QQPVRLRDVR
ALFLDSGISQ NSLAIISQGR VDQILNSQAR ERRGIFEEAA GVLHFKQQKQ QAQRQLETTN
DNLIRINDLV NELEKRLEPL HEQSSLAQEY QFQKAALDED LKTLLAFEIA DLDQEEREVS
QKLAKSQELL SRLDAEVKQS QAKLAAKRQE FQLESQKRDQ VQAEVLKLTN RLSEINTSLQ
VSQQSRQFDQ ATRLEYQRQL ADLKENLAAT DAEISKLADQ EAEYAGQLDQ LKCKRQKLVD
QLKEDPASLK LKVEDLRSQY IQTLQDQTSV NNQLVYLEGE IKRAKESKDQ RYEDASSQLA
KSQEELEGLR LKEQKLRAEN DQLQAELKEA SDQLGKLAAE QQVAQKQLQA DLTNLQRLTA
RRDALVNIQK RHDGYYAGVK QVLNQPDRFP GIIGAVGELL TFPADLEAAM TTALGGNVQS
LVAKDRMAAK DAIQQLKVRR LGRATFLPLD ALRYRAIPAS TRQALERFAG FQGLASELVE
AKGDTDISEA IQYLLGSIII VDNMDTALAV SRQIGHYRVV TLDGDVISPG GAMTGGARNQ
RNNSPLQTTA EINKTTAMLE ELERQFHIKE EKLAGLDKQV KDKQENREQI SRDLQSLQQD
LSAAVLTFQS QEKEVKRLES AVQLYQAQQA EQAAYLADLT DKEKAQKIKK EELAALADQQ
KRDLASLQET IQNYTDLNQG VQEKLAELDP QLAVLANKQE NLQARKAELG RQKAAIQKQI
GQLEEKLAAL DNSSQLSARK KEELGLEKDR LLAEQKDKQA DLDAASQLLG QLNGQINQLE
AVATRNYDLR KDAASEQEEL SVKLATVKGQ LKQHLDSLRE DYSLTYEAAL SQAKLENTEE
NQQNLRRSVK LHRMSLEDIG PVNLGAIDEY KEVKDRYDFL NGQQNDLLEA RSNLQQSMDE
LDQEVKGRFG QTFQQISASF SRLFPVVFGG GNARFTLTDP DNLLESGVEI IAQPPGKKLQ
RLSLLSGGER SLTAITLLFA MLEVNPVPFC VLDEVEAALD DANVARFARF LRQYDSQTQF
IVITHRRGTM EQADQLYGVV MQESGVSQIL SVSLKDLKDE V
//
