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Database: UniProt
Entry: F0EGI8_ENTCA
LinkDB: F0EGI8_ENTCA
Original site: F0EGI8_ENTCA 
ID   F0EGI8_ENTCA            Unreviewed;      1192 AA.
AC   F0EGI8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
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:EGC70908.1};
GN   ORFNames=HMPREF9087_0285 {ECO:0000313|EMBL:EGC70908.1};
OS   Enterococcus casseliflavus ATCC 12755.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=888066 {ECO:0000313|EMBL:EGC70908.1, ECO:0000313|Proteomes:UP000004835};
RN   [1] {ECO:0000313|EMBL:EGC70908.1, ECO:0000313|Proteomes:UP000004835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12755 {ECO:0000313|EMBL:EGC70908.1,
RC   ECO:0000313|Proteomes:UP000004835};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGC70908.1}.
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DR   EMBL; AEWT01000002; EGC70908.1; -; Genomic_DNA.
DR   RefSeq; WP_005232485.1; NZ_GL872323.1.
DR   AlphaFoldDB; F0EGI8; -.
DR   HOGENOM; CLU_001042_2_2_9; -.
DR   Proteomes; UP000004835; Unassembled WGS sequence.
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; 1.20.1060.20; -; 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; 2.
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|HAMAP-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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}.
FT   DOMAIN          518..637
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          167..201
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          255..345
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          427..468
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          672..860
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   1192 AA;  134909 MW;  83EBBB5C39781EE1 CRC64;
     MYLKRIEIAG FKSFADRTVI DFEHRVTAVV GPNGSGKSNI TEAIRWVLGE QSAKNLRGGK
     MPDVIFAGSD TRRALNIAEV TIVLDNSDHY LPMDYSEISV TRRLRRTGES DFFLNKQACR
     LKDIQELFMD SGLGKESFSI ISQGKVEAIF SSKPEDRRGI FEEAAGVLKY KQRKKKAEQK
     LFETEDNLSR LQDIIYELED QLVPLAAQSD AANRFLALKE KLTTVDVAYA VLEITKAKEA
     WETAKAQLST FNQELAQISE KINQGELSLH SLRQQRTAFD ETLERLNQQL LEVTEGLKQA
     EGQKEVLDER SKHTQKSSAE YQETLEEVTE RVTLLNEEKA ELIGLLSQKN RSVQEVEAAM
     LACQQEQEKY QRSAKEIIEE LRSQYVEAMQ EQATIGNELK YLERQYQQEA AKNQTALSKQ
     TQMNTSLKEK TMEAQIVEEQ LTQAKAILEE QRKQYIHLQE KAQTNKKRFD EEQKKMYQLM
     SQVQQVRAKQ RSLQDIQENY SGFYQGVRLI LKNKQQISGI VGAVAELIDV PQDYTVAIET
     ALGAAAQHVV VENERDARAA ITYLKENRGG RATFLPLTTI KARHLPDYAR NQAKQVSGFI
     GVASELVQSP EHIQTITDNL LGSILIAEDL QSANALARAL NYSYRVVSLE GDVMNAGGSM
     TGGATKKNAG SLFSQSNELQ QLTAQAAQLD ERLLKTEKQV QHFEAATKEA QAALEELRTQ
     GEQARMTEHE LQSRLKNLEN DLSRLKQEQQ VFDFEHREVQ AFFEEYDEKK TSLEEQQKNI
     AAQLAKIDQD IHQMNAEEDL IEEKRQTLAQ ESARLQAAFA VQKEQVAHLQ QKIAATNQAL
     EENEARQHSL ERQLAALTSN VSDHEFSEEN ILQRIEAFTK TKQQVTAELT VIREQRQVVQ
     QEIGALDEAL SAENLTQKEK LSEKTEVEIE KNRAELVMDN RLLYLQEEYN LTFEKAAQDF
     PEIEDAEQAK IDIQELKHAI EQIGPVNLNA IEQYEQVNQR HLFLTSQRDD LLSAKAQLFD
     TMSEMDEEVK TRFGEVFDAI RLQFKQVFPN MFGGGHAELV LTDPKDLLNT GIEIEAQPPG
     KKLQNLSLLS GGERALTAIA LLFSIIQVRP VPFCVLDEVE AALDEANVSR FGHYLSAFQN
     DTQFIVVTHR KGTMEAADVL YGVTMQESGV SKTVSVRLEE VREGGSFAAD QA
//
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