ID   SMC_SYNP6               Reviewed;        1195 AA.
AC   Q5N0D2;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=syc2048_d;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAD80238.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP008231; BAD80238.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041677034.1; NC_006576.1.
DR   AlphaFoldDB; Q5N0D2; -.
DR   STRING; 269084.syc2048_d; -.
DR   EnsemblBacteria; BAD80238; BAD80238; syc2048_d.
DR   KEGG; syc:syc2048_d; -.
DR   eggNOG; COG1196; Bacteria.
DR   Proteomes; UP000001175; 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; 2.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF75553; SSF75553; 1.
DR   TIGRFAMs; TIGR02169; SMC_prok_A; 1.
DR   TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding.
FT   CHAIN           1..1195
FT                   /note="Chromosome partition protein Smc"
FT                   /id="PRO_0000409281"
FT   DOMAIN          542..658
FT                   /note="SMC hinge"
FT   COILED          185..241
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          273..348
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          380..528
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT   COILED          698..1043
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   1195 AA;  135269 MW;  F7328DF2D2DC8E4D CRC64;
     MVYIKQIELS HFKSFGGTTS LPLLPEFTVV TGPNGSGKSN ILDALLFALG LSSSKGMRAD
     RLPDLVNSTY ASRSRSTVET LVTVTFALDD WQPEAEETEE GEGTGLQPGM AEWTVSRKLR
     VTPSGTYTST YAMNGEACTL QQLHEQLSRL RIYPEGYNVV LQGDVTNIIS MSPRDRRQII
     DELAGVAQFD RKIEQAKGKL EAVKEREDRC RIVEQELIEQ RDRLAKDREK AQKYQALRQE
     QATKQSWEAV LRWRAGQRQV QALQRSLAQL ATDAATDQQT QQTLEQQIQQ TEATLDRLNQ
     RVKALGEEEL LKLQAALAQQ EAEQRQSQRQ QQELVESQTQ TQQQIQALLQ TQAQLQTEGQ
     QQAEQARTLQ TTIAQTLQPQ YQQALEQVEA ARQSAHALAA QSQDWVTRQT SLRQQADAIA
     AQVEPQRAEQ AQLQERQTQL QQQLEATQSA LVTVTAELET ETEQAEGDRA ALSQAEAAVV
     TAADQLVRLE EELQIQQETR DRLLKEQRDK QRQLDRQESL RQAMQETQGT AAARLILDTG
     LPGVHGLVAQ LGRVEPRYQL ALEVAAGGRL GYLVVDDDGV ASAGIELLKQ KKAGRITFLP
     LNRIRAGKQP EIPRWQQPEG LVDLAIALVD CDDRYREVFK FVLGGTVVFE RLDQARRYMG
     QYRIVTLDGE LLETSGAMTG GSIARRSGGL SFGSPDSGES AEVRAIRDRL EQLEVILDRS
     ELQILNLQAA IKDAASTLSD RRQQQREQQL TVQQRQQTLQ RLQQQQQQLN AELQQRQQQA
     SQAQARLAAL ALELPAALKQ LKTLRQALAE LEDSPIHGEW QQRQTLLQQQ EALLQQQETA
     LRQAEQQLQQ LQTDQKRLQE RAIAARTQVS QLRQQQGEQL NRLAQLDEQQ RQQATAIAQL
     QQRQAQLEAQ LGQEKVDRDR TERQLQEQRS QRQNLVWQQE KRQQQQQELQ QQLTDLEVQL
     QAEQQELPQP LPDIPEMVQQ QGIEALQHEL RSLAKRIQAM EPVNMLALEE YERTQARLEE
     LSEKLTTIEA ERTELLLRIE NFTTLRRRAF MESFEAIDRN FQEIFAHLSD GDGSLQLDNP
     EDPFSSGLNL IAHPKGKPVR RLASMSGGEK SLTALSFIFA LQRYRPSPFY ALDEVDSFLD
     GANVERLARV IRQQAQAAQF IVVSHRRPMI EAAERTIGVT QARGAHTQVL GIPQP