ID E4SKB3_LACAR Unreviewed; 1189 AA.
AC E4SKB3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 01-MAY-2013, entry version 17.
DE RecName: Full=Chromosome partition protein Smc;
GN Name=smc; OrderedLocusNames=LA2_07325;
OS Lactobacillus amylovorus (strain GRL 1112).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=695560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GRL 1112;
RX PubMed=21131492; DOI=10.1128/JB.01365-10;
RA Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.;
RT "Genome sequence of Lactobacillus amylovorus GRL1112.";
RL J. Bacteriol. 193:789-790(2011).
CC -!- FUNCTION: Required for chromosome condensation and partitioning
CC (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: Contains large globular domains required for ATP
CC hydrolysis at each terminus and a third globular domain forming a
CC flexible hinge near the middle of the molecule. These domains are
CC separated by coiled-coil structures (By similarity).
CC -!- SIMILARITY: Belongs to the SMC family.
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DR EMBL; CP002338; ADQ59386.1; -; Genomic_DNA.
DR RefSeq; YP_004032181.1; NC_014724.1.
DR EnsemblBacteria; ADQ59386; ADQ59386; LA2_07325.
DR GeneID; 10023429; -.
DR KEGG; lam:LA2_07325; -.
DR PATRIC; 43077908; VBILacAmy150400_1444.
DR HOGENOM; HOG000036392; -.
DR KO; K03529; -.
DR OMA; NNEVHAL; -.
DR BioCyc; LAMY695560:GI0Z-1511-MONOMER; -.
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:HAMAP.
DR GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:HAMAP.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR HAMAP; MF_01894; Smc_prok; 1; -.
DR InterPro; IPR003395; RecF/RecN/SMC.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR011890; SMC_prok.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 2.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF75553; SMC_hinge; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Complete proteome; Cytoplasm; DNA-binding;
KW Nucleotide-binding.
FT NP_BIND 32 39 ATP (By similarity).
FT COILED 167 492 By similarity.
FT COILED 671 907 By similarity.
FT COILED 1005 1033 By similarity.
SQ SEQUENCE 1189 AA; 134689 MW; 3A989545D0729E13 CRC64;
MPLTELVLDG FKSFAEKTTI HFNDGITGIV GPNGSGKSNI TEAIRWVMGE SSAKSLRGTN
MKDVIFAGSQ YRKPLNKAEV TLVFDNKDRE LAFDADQVSI TRRILRSGDS EFLINNQQVR
MRDVRALFLD SGISPNSLAI ISQGRVDQIL NSRPEQRRLI FEEAAGVLHF KQQKEEAQTQ
LKKTQDNLIR INDLVKELEG RLEPLHEQSS LAKEYQFQKA GLDKKLKSLL AFEIEDINRQ
KEDVEKSAKK SQVLLSKLDN EVKDSQDAVS EKRGEYKKLQ TERDNTQKQL LELSKKLSDL
DASLQMAEQS RQFDDATKVE YQNQVKSLKN SLVKLNEDLA SLQKNATELK DKQAVLQKQR
DELTAELKED PEELNKKLES CRNDYIQLLQ DQATTNNQIV NLNTELKRSK ADTSYQNSDV
SKQLSEAKTE LEKLRAEGKT LTEKRKSEKI KLAEVGDQNS DLTNKVNQLR QTVANERGKL
EKIEARHEAL VNIQKRHEGY YYGVRNVLNN MNAFPGVIGA VGELISFPVE LEAAMTTALG
GGVQDLITDS RISARNAINQ LKRNRAGRAT FLPLDGLRQY GIPQSTVTTL ESYEGFRGVA
SDLVESKTEH NINAAINYLL GSVIIVDTID TALSISKRIN RYRIVTLDGD VISPGGSMTG
GQRNQRNNSP LQTATEINQL EAQIKTLTKT LREDQNQLET LVDQAQRANA ELQKLQSSLQ
ETNQAINEVA ISFQSQEKEV KRLTDANNLY ESRIKERDSR IKELKQQIEE AQTKQNELTK
QGKEQRTAMN QLQERIRNFN SLSQKVQDQL SKLDPDIAVY TNKLENLRSQ ENEKKQQIRN
NQEQTADLTH KLQDLTQSGE RSVQKNTDLK KQKADLKQQT EDLQTKLNEL SSQLGQFDAQ
INQLDQVASR NYELRKDAAI EQEGYSVQLA KFNSAINQRL ETLRDDYSLT YEAALAQAEG
ENDEDTRNEL AKSVKLHRMS IEDIGPVNLD SIQEYEDVKK RYDFLSGQQN DLLKARDDLE
KSMNELDEEV KTRFKDTFNT IADSFKQIFP VVFGGGKAKL ELTEPNNLLE TGIEIIAQPP
GKKLQRLSLL SGGERALTAI TLLFAMLQVN PVPFCVLDEV EAALDDANVT RFAQFLLKYD
MKTQFIVITH RRGTMRKADQ LYGVVMQESG VSQVLSVSLK ELKNKHEVR
//