ID K9RTG1_SYNP3 Unreviewed; 1191 AA.
AC K9RTG1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Syn6312_1598 {ECO:0000313|EMBL:AFY60758.1};
OS Synechococcus sp. (strain ATCC 27167 / PCC 6312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=195253 {ECO:0000313|EMBL:AFY60758.1, ECO:0000313|Proteomes:UP000010379};
RN [1] {ECO:0000313|Proteomes:UP000010379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27167 / PCC 6312 {ECO:0000313|Proteomes:UP000010379};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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 Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; CP003558; AFY60758.1; -; Genomic_DNA.
DR RefSeq; WP_015124302.1; NC_019680.1.
DR AlphaFoldDB; K9RTG1; -.
DR STRING; 195253.Syn6312_1598; -.
DR KEGG; syne:Syn6312_1598; -.
DR PATRIC; fig|195253.3.peg.1624; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_3; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000010379; 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 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; TIGR02169; SMC_prok_A; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 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; 2.
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|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000010379}.
FT DOMAIN 547..661
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 93..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..525
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 729..815
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 856..960
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 95..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1191 AA; 136383 MW; D9E334DDA18AB787 CRC64;
MYVKQLELTN FKSFGGTTAI PLLPGFTVVS GPNGSGKSNL LDALLFALGL AGSKGMRAER
LPDLVNHSQT RRNQSVVETR VVVTFALEPH EIPQATLSTE DSPAPPTESS AHPQTLEWQV
TRKLRVTKQG TYTSTYLLND QACTLNELHN QLQQLRIYPQ GYNVVLQGDV TGIISMNSKQ
RREIIDELAG VADFDRKINQ AKEKLDTVKE REERFRIVEQ ELIQQRDRLQ RDRVQAEKYK
VLRQELETKQ EWSRVLAWAT VQRQIKQLQT QIKEGEKSQT QLQTQLEQLT TQINTDTKTL
ETLNRQVKAL GEDELIKLQT QLAQKQAEQR QLERQQTELK QTQLHQAEEL RNLQITLATE
QTQLETLKKQ QQQLETEQIQ PQHQACQIAL QELEASRNQA KTLNAAAQAW MQEHTQIRQE
INQLATQLEP QRLEQSRLQE RQSQLERQIS EQTQALAEIE SELAIVEDEM ATADTLLAPE
QAEIQRLAQQ IAQLQEQLHL NQQTRDRLHR EQRDKQRQLD KLEAQQLAIQ ETQGTQATRL
ILQAQLPGVI GTVAQLGRVE TAYQLALEIA AGGRLGQIVV EDDSVAAAGI EILKRERGGR
ATFLPLTKMQ SPRNLPNLNL PGLVDYALNL IEFERRLLPI FAYVFGQTLV FEDLATARRY
IGQHRIVTLD GELLETSGAM SGGSRSQQSS LHFGKSEAQE SNEVRELRHR LAEIDRLLGR
IETDISSQQV KLQKKIQDLT EKREQLRDLD QQQNQLKTSA QALTRQQQQI QTQLSQNQSE
LSVTLAKFHQ LTTDLPQQET RLSQLRETLA KLEESQTHNE WQTLQDQVQQ KEQAWQTQDA
TLRGLERQKQ DLIYHYQRQE TQIQQHQTRI ATLQQQQTQA LQQATQSETE ISQVLAQVNE
LEKQIRGLET QMGEIKQQRD QQEYQLRQAQ TQQQSLQWQL QNLTETQAQK QTELKSLTEQ
TPPELPPELP EIPADLTLPQ LQEQILNLEK RLRAMEPVNM RAIEEYEHTQ TRLDELSQKL
GVLDSERTEV LLRIENFTTL RHQAFQEAFD AVNINFQAIF ATLSDGDGYL QLENAQDPFA
GGLNLVAHPK GKPVQRLASM SGGEKSLTAL SFIFALQRYR PSPFYAFDEV DMFLDGANVE
RLSRMIQQQA QQAQFIVVSL RRPMIEASQR TIGVTQARGQ HTQVIGIKLQ D
//
