ID B2HJJ8_MYCMM Unreviewed; 1200 AA.
AC B2HJJ8;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
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:ACC40234.1};
GN OrderedLocusNames=MMAR_1785 {ECO:0000313|EMBL:ACC40234.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC40234.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC40234.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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}.
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DR EMBL; CP000854; ACC40234.1; -; Genomic_DNA.
DR RefSeq; WP_012393589.1; NC_010612.1.
DR AlphaFoldDB; B2HJJ8; -.
DR STRING; 216594.MMAR_1785; -.
DR KEGG; mmi:MMAR_1785; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_11; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000001190; 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; 2.
DR Gene3D; 1.10.287.1490; -; 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; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW 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|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT DOMAIN 510..624
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 174..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 262..289
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 340..374
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 459..486
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 975..1023
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 1200 AA; 130627 MW; 792E8D2F533E7C8E CRC64;
MYLKSLTLKG FKSFAAPTTL RFEPGITAVV GPNGSGKSNV VDALAWVMGE QGAKTLRGGK
MEDVIFAGTS SRAPLGRAEV TVTIDNSDNA LPIEYTEVSI TRRMFRDGAS EYEINGSSCR
LMDVQELLSD SGIGREMHVI VGQGKLDEIL QSRPEDRRAF IEEAAGVLKH RKRKEKALRK
LDAMSANLAR LTDLTTELRR QLKPLGRQAE VARRAQTIQA DLRDARLRLA ADDVVSRRAE
REAIFEAEAT MRREHDEAAA RLTVAAEELA AHEAALAELT SRAESVQHTW FGLSALAERV
GTTVRIANER AQHLDVEPVT NSDTDPDALD AEAEQVAIAE QQLLVELAEA RDRLDAARAE
LADREHRAAE ADRAHLAAVR AEADRREGLA RLAGQVETMR ARVESIDDSV ARLSERIEHA
AARAQQTRAE FETVQARVGE LDQGEVGLDE QHERTVAALR LAEQRLAELQ VAERDAERQV
ASLRARIEAL SVGLDRKDGA AWLARNHSDA GLFGSVAQLV KVRSGYEAAV AAVLGSAAEA
LAADSFGAAR SAVTALKQAD GGRAALVLGD WPDANDHRAA GGLPSGTLWA LDLIEVPSRL
RPAMTAMLSG VVVVNDLSEA LDLVQAQPQL RAVTLDGDLV GAGWVSGGSD RKPSTLEITS
EIDKARSELA AAEVRVAELG AALSGALTDQ TARQDAAEQA LAALNESDTA ISAMYEQLGR
IGQDARGAEE EWTRLLRQRE ELEVGRTQTL EEVLELESRL RNAQESQHVQ AAEPVDRQEI
AAAAESARAI EVEARLTVRT AEERANALRG RADSLRRAAA AEREARVRAE LARAVRLRSA
AVAAAVAESG RLLAWRLNRV VDAASQLRDE LAAERQQRSA AMSAVREETS SLSARVATLT
DSLHRDEVAN AQAALRIEQV EQMVLEQFGM APSDLVAEYG PDVALPPTEL EMAEFEQARE
RGEQVVAPAP MPFDRATQQR RAKRAERELT ELGRVNPLAL EEFAALEERY NFLSTQLEDV
KAARKDLLDV VADVDARILQ VFSDAFVDVE REFQIVFSSL FPGGEGRLRL TAPEDMLTTG
IEVEARPPGK KVSRLSLLSG GEKALTAVAM LVAIFRARPS PFYIMDEVEA ALDDTNLRRL
IGLFEMLRDR SQLIIITHQK PTMEVADALY GVTMQGDGIT AVISQRIRGQ QVDRLVANSS
//
