SMC_MYCGE
ID SMC_MYCGE Reviewed; 982 AA.
AC P47540; Q49301;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
DE AltName: Full=Protein P115 homolog;
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=MG298;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 915-981.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L43967; AAC71520.1; -; Genomic_DNA.
DR EMBL; U02177; AAD12461.1; -; Genomic_DNA.
DR PIR; I64232; I64232.
DR RefSeq; WP_010869416.1; NC_000908.2.
DR AlphaFoldDB; P47540; -.
DR SMR; P47540; -.
DR STRING; 243273.MG_298; -.
DR EnsemblBacteria; AAC71520; AAC71520; MG_298.
DR KEGG; mge:MG_298; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_14; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 1149850at2; -.
DR BioCyc; MGEN243273:G1GJ2-367-MON; -.
DR Proteomes; UP000000807; 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; PF06470; SMC_hinge; 1.
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.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..982
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000119025"
FT DOMAIN 416..535
FT /note="SMC hinge"
FT COILED 171..231
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 280..310
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 337..377
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 575..718
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 753..822
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT CONFLICT 975..982
FT /note="YVSENDSN -> ICIWKWF (in Ref. 2; AAD12461)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 982 AA; 111073 MW; E31CA2430B895A87 CRC64;
MVFLKRFRAY GFKSYADEIT IDFTHSMTGI VGPNGSGKSN VVDALKWVLG ERSMKHLRSK
SGDDMIFFGS KDKPASKLAE IELTFDNSNR LLHDSRKEIS VMRRVYRGSG QSEYFINSNP
ATLKEISGIF ADIGLEKGSL GIISQGSVSW FVEAKPEERR KIFEDASGIG RYTKRKEEVV
NQLNRTLINL KQVSVVLNEL KKDLKKLTLQ AEKAQQFIRV KNELKELELA VLVGEYLQAQ
TELDKFNFQI NSSEHDFKIH EPQLELLEEQ IVIFNSRFHS ADMQSNELQK ELQDIYQKIN
ELEQRKVIID VQLRQGFSQK DEKQKAAALK KLILVDQTQL DGFENQLSNS KTTITDLEKL
INEQKSLVDQ IKLQIEKNTA DLIYQRSLKT IIELQTNELK KTNNANILVK NANALTGILN
TLGTFLKFDK QYEKAILKAL GKSIGYLVVN NNNAAIQAID FLVKNEIGKV TFLPLDDVAS
DTKITNEHME ILKQLDGFLG VCSDHVKCDP LFQPVVNTLL AQVIIAKDLN SAINLSNYTY
KLYRIVTLDG ETVYAGGIIN GGFEKTNLSD GYLSSASLDN EQNINKLENN ERELKKELTE
LEVKLDEMNR KLKYEELLQA KFIERIVQIK KIILELKMEY EQLTNTTFDG KKAVASEAEL
IHSLNSAWAK RDEINSKLKL NQELKLQLAK TIKQSEEKIV DLRALLDEQR AKLVSAREGK
IRFENTIQNI TEKINSVYKM TMEFAIANHN KPVKLSSMQA HNKIAKLQNQ LNEMGVINME
SIAEISEKQK RFDDINAEYE SAQQAVENLQ KAITEIDEIA SNEFDQLIQK LNQELPKTFK
YLFGGGSCQI RYTDPSNVLV SGIDVFANPP GKNIANLMLL SGGEKTLVAL SVLFSILKVS
AFPLVILDEA ESALDPANVE RFANIIKTAS KNTQFLIITH RQGTMMKCDM LLGAAMQTKG
VTKTFAVELE NAEKYVSEND SN