ID SMC_MYCTU Reviewed; 1205 AA.
AC P9WGF3; L0TCM4; Q10970;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=Rv2922c;
GN ORFNames=MTCY338.11c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 SMC hinge
CC near the middle of the molecule. These domains are separated by coiled-
CC coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; AJ414609; CAC93884.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45724.1; -; Genomic_DNA.
DR PIR; B70748; B70748.
DR RefSeq; NP_217438.2; NC_000962.3.
DR RefSeq; WP_003899542.1; NZ_NVQJ01000006.1.
DR AlphaFoldDB; P9WGF3; -.
DR SMR; P9WGF3; -.
DR STRING; 83332.Rv2922c; -.
DR PaxDb; 83332-Rv2922c; -.
DR GeneID; 887179; -.
DR KEGG; mtu:Rv2922c; -.
DR TubercuList; Rv2922c; -.
DR eggNOG; COG1196; Bacteria.
DR InParanoid; P9WGF3; -.
DR OrthoDB; 9808768at2; -.
DR PhylomeDB; P9WGF3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; 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: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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1205
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000119030"
FT DOMAIN 514..628
FT /note="SMC hinge"
FT COILED 169..288
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 330..499
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 661..771
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 802..836
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 979..1033
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 1205 AA; 130637 MW; A3B2A813B58EACF3 CRC64;
MYLKSLTLKG FKSFAAPTTL RFEPGITAVV GPNGSGKSNV VDALAWVMGE QGAKTLRGGK
MEDVIFAGTS SRAPLGRAEV TVSIDNSDNA LPIEYTEVSI TRRMFRDGAS EYEINGSSCR
LMDVQELLSD SGIGREMHVI VGQGKLEEIL QSRPEDRRAF IEEAAGVLKH RKRKEKALRK
LDTMAANLAR LTDLTTELRR QLKPLGRQAE AAQRAAAIQA DLRDARLRLA ADDLVSRRAE
REAVFQAEAA MRREHDEAAA RLAVASEELA AHESAVAELS TRAESIQHTW FGLSALAERV
DATVRIASER AHHLDIEPVA VSDTDPRKPE ELEAEAQQVA VAEQQLLAEL DAARARLDAA
RAELADRERR AAEADRAHLA AVREEADRRE GLARLAGQVE TMRARVESID ESVARLSERI
EDAAMRAQQT RAEFETVQGR IGELDQGEVG LDEHHERTVA ALRLADERVA ELQSAERAAE
RQVASLRARI DALAVGLQRK DGAAWLAHNR SGAGLFGSIA QLVKVRSGYE AALAAALGPA
ADALAVDGLT AAGSAVSALK QADGGRAVLV LSDWPAPQAP QSASGEMLPS GAQWALDLVE
SPPQLVGAMI AMLSGVAVVN DLTEAMGLVE IRPELRAVTV DGDLVGAGWV SGGSDRKLST
LEVTSEIDKA RSELAAAEAL AAQLNAALAG ALTEQSARQD AAEQALAALN ESDTAISAMY
EQLGRLGQEA RAAEEEWNRL LQQRTEQEAV RTQTLDDVIQ LETQLRKAQE TQRVQVAQPI
DRQAISAAAD RARGVEVEAR LAVRTAEERA NAVRGRADSL RRAAAAEREA RVRAQQARAA
RLHAAAVAAA VADCGRLLAG RLHRAVDGAS QLRDASAAQR QQRLAAMAAV RDEVNTLSAR
VGELTDSLHR DELANAQAAL RIEQLEQMVL EQFGMAPADL ITEYGPHVAL PPTELEMAEF
EQARERGEQV IAPAPMPFDR VTQERRAKRA ERALAELGRV NPLALEEFAA LEERYNFLST
QLEDVKAARK DLLGVVADVD ARILQVFNDA FVDVEREFRG VFTALFPGGE GRLRLTEPDD
MLTTGIEVEA RPPGKKITRL SLLSGGEKAL TAVAMLVAIF RARPSPFYIM DEVEAALDDV
NLRRLLSLFE QLREQSQIII ITHQKPTMEV ADALYGVTMQ NDGITAVISQ RMRGQQVDQL
VTNSS
//
