SMC_XANOR
ID SMC_XANOR Reviewed; 1167 AA.
AC Q5H054;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=XOO2413;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW75667.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE013598; AAW75667.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011408596.1; NC_006834.1.
DR AlphaFoldDB; Q5H054; -.
DR STRING; 291331.XOO2413; -.
DR EnsemblBacteria; AAW75667; AAW75667; XOO2413.
DR KEGG; xoo:XOO2413; -.
DR PATRIC; fig|291331.8.peg.2684; -.
DR HOGENOM; CLU_001042_2_2_6; -.
DR Proteomes; UP000006735; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1167
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409285"
FT COILED 170..274
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 310..390
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 468..500
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 653..870
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 982..1011
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1167 AA; 130072 MW; 63A084291A07810D CRC64;
MRLSTIKLSG FKSFVDPTTL HLPTNMTGIV GPNGCGKSNI IDAVRWVMGE SSASRLRGDS
LTDVIFSGSS ARKPVSQATV ELIFDNSDHT ISGEFASFNE ISVKRLVSRD GNSAYYLNGT
KCRRRDITDL FLGTGLGPRS YSIIEQGMIS QIIEARPEDL RVYLEEAAGI SKYKERRKET
ETRIRHTREN LDRLGDLREE ITKQLAHLQR QARQAEQYQA LQEERRIKDA EWKALEYRGL
DGQLQGLREK LNQEETRLQQ FIAEQRDAEA RIETGRVRRE ESAEAVAKAQ ADVYQVGGAL
ARIEQQIQHQ RELSHRLHKA RDEAQSQLQE LTQHISGDSA KLSVLREAVA AAEPQLEQLR
EDHEFRQESL REAEARLADW QQRWETHNRD TGEASRAGEV ERTRVDYLDR QALEADRRRE
ALVNERAGLD LDALAEAFEQ IELRHETQKT SLDGLTEQVE ARKHALGGLQ EQQRASQGEL
AEVRKQAQAA RGRLSSLETL QQAALGQEQG AAVAWLKSRG LDSAARVGER ISVQSGWENA
VEGALGQLIE GVLVDAPEQL VDALGELGDG RIALVSSATD NANFAPTSLA AKVQGPIAIR
RLLARLHTAE DLDAARTLQR SLPEGDSVIT RNGERLGEGW VRVSRSGAAK QGALLRERQI
QELRTQIETL QEREAELEHQ LASFREQLLA AEQQREDAQR QLYMAHRSVS ELAGQLQSQQ
GKVDAARTRI ERIETDLSQL LETLDTSREQ AREARAKLED AVTLMGDLQG TREALESERR
QLTDARDQAR DAARGVRDAM HALALTLESQ RTQIASLSQT LERMDSQRGQ LDTRLEDLVA
QLSEGDSPVE TLEHEHQAAL SERVRTERAL GEARTLLDSI DSELRSFEQT RQQRDEQALA
QRERISQRKL DQQALVLSAE QLSAAVVKAG FVLEDVVNGL PESANPAEWE ATVGQIDGRM
RRLEPVNLAA IQEYGEAAQR SEYLDAQNLD LNTALETLEE AIRKIDRETR GRFKDTFDRV
NSGVQALYPR LFGGGHAYLE LTGEDLLDTG VTIMARPPGK RVSSISLLSG GEKAMTAVAL
VFAIFQLNPA PFCLLDEVDA PLDEANVGRL ANMVREMSEK VQFLFVSHNK ATMEAARQLS
GVTMREPGVS RLVSVDLEEA ARLAGAA