SMC_MYCPN
ID SMC_MYCPN Reviewed; 982 AA.
AC P75361;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
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}; Synonyms=p115;
GN OrderedLocusNames=MPN_426; ORFNames=MP415;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96063.1; -; Genomic_DNA.
DR PIR; S73741; S73741.
DR RefSeq; NP_110114.1; NC_000912.1.
DR RefSeq; WP_010874782.1; NC_000912.1.
DR AlphaFoldDB; P75361; -.
DR SMR; P75361; -.
DR IntAct; P75361; 3.
DR STRING; 272634.MPN_426; -.
DR EnsemblBacteria; AAB96063; AAB96063; MPN_426.
DR KEGG; mpn:MPN_426; -.
DR PATRIC; fig|272634.6.peg.461; -.
DR HOGENOM; CLU_001042_2_2_14; -.
DR OMA; HNKIAME; -.
DR BioCyc; MPNE272634:G1GJ3-689-MON; -.
DR Proteomes; UP000000808; 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; 2.
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_0000119027"
FT DOMAIN 416..535
FT /note="SMC hinge"
FT COILED 171..235
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 263..377
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 568..627
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 669..713
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 753..818
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"
SQ SEQUENCE 982 AA; 110833 MW; C9D5F765B752E228 CRC64;
MVFLKRFRAY GFKSYADEIT INFTHSMTGI VGPNGSGKSN VVDALKWVLG ERSMKHLRSK
SGDDMIFFGS KDKPASKLAE VELTFDNSQK LLHDPRPEIS VMRRIYRGSG QSEYYINGEL
VTLKEISGIF ADIGLEKGSL GIISQGSVSW FVEAKPEERR KIFEDASGIG RYTKRKEEVT
NQLARTVQNL KQVSIVLNEL KKDLKKLTIQ ADKAQRFVKL KEELKELELS VLVADYLKSQ
GELDRFNHQI GYIEQDFKLH EPQLQLLEDQ LNIFNQRFRD ADEQSIKLQQ ELQAVYQTIN
ELEQRKAVID VQLKNELSKK DEKHKIQALK KLIRVDQAQL ESLQAQVLKT TSEITLLTNE
LSTVQTELDT TKLNLNQNSA ALVYQQAQQE FLKAQNEEWV KTNPAHVLVK NVKALTGLLN
TLNTFLKFEK QYEKALLKAL GKSIGYLVVN NNLAALKAID FLLTNQIGQV TFLPIDDIAF
DTKIAPEHME ILQQLDGFLG VGSDHVSCDE SLQPIVNALL GQVIIASDLQ AALKLSSYTY
KLYRVVTLNG ETVYAGGIIQ GGYVKDNLSL YNLQEKLASS EANITQLEHN EKQLRTNLTS
LETKLNELNK KLKYEEILLE KFNERVNHTN KAILSYKIEY EQLTNESFDG TPHSFDETRL
VESLNRAWAE RDELNSQLKL NQELKETLAK SIKLAEAKTA DLRALLDEQR SQLVLAREGK
IRFENTIHNI TDKINGGYKL TMEFAIANYN KPIKLSTMQA QNKIARMQSQ LDEMGPINLE
SIAEIADKQK RFDDINGEYE SLQTAIKDLQ TAIGEIDELA CKEFDELIQK VNAELPKTFN
YLFGGGSCQI RYTDTDNVLL SGIEVFANPP GKNVANLMLL SGGEKTLVAL SVLFSILRVS
AFPLVILDEA ESALDPANVE RFANIIGNSS NNTQFLIITH RQGTMMKCDM LLGAAMQTKG
VTKTFAVSLE KAEQYISKDK QN
