SMC_GLOVI
ID SMC_GLOVI Reviewed; 1165 AA.
AC Q7NG51;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=glr3322;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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}.
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DR EMBL; BA000045; BAC91263.1; -; Genomic_DNA.
DR RefSeq; NP_926268.1; NC_005125.1.
DR RefSeq; WP_011143312.1; NC_005125.1.
DR AlphaFoldDB; Q7NG51; -.
DR SMR; Q7NG51; -.
DR STRING; 251221.35213893; -.
DR EnsemblBacteria; BAC91263; BAC91263; BAC91263.
DR KEGG; gvi:glr3322; -.
DR PATRIC; fig|251221.4.peg.3353; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_3; -.
DR InParanoid; Q7NG51; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 1149850at2; -.
DR PhylomeDB; Q7NG51; -.
DR Proteomes; UP000000557; 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.
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;
KW Reference proteome.
FT CHAIN 1..1165
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409273"
FT DOMAIN 518..630
FT /note="SMC hinge"
FT COILED 161..503
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 672..901
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 946..1010
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1165 AA; 131255 MW; D5033954A657DEA5 CRC64;
MHLKCLEIER FKSFGPYTRI PLLEGFTVVS GPNGSGKSNI IDALLFALGL STSRGMRAEK
LSDLIHQGAA KGEVAVTVTF ALDAAAGGGE LTVCRRLKVN GPNSTSSYQL NGSPCTLTDL
HEELARHHIY PEGYNVVLQG DVTGIIAMPA RERREIIDEL AGVAEFDRKI EAARRELGEV
EVRSDRIQAV VSELLEQMER LQKERAKAEE YRKLRAELGE LALWEHLLSV RSLEAQIAQI
TSQLAAAEAV LAGFDREAEA LAERCEQALD ELDTANTRVK AMGENEQVAL RTQMASVQAQ
RAQAEAALAD LAQQQRQAQG RQQQLELELG ELALTLTGFS RRQQDQQALV AQWTARLESD
RQVLETSRND LEQLSASSRR WVEEQSQLRR RLDQLQSEHD PLQRTLDRLG DRLVQATGEG
ERHREELARI EAGHAQLATE AKVAQERLAA ARTRLEQTRA DLEAERAQIL ADRTTQRRLE
KERTEKAREL DRLETQRQVW REAEGSRATQ EVLGSGIQGV HGLISQLGRV EAQYQGALEV
AAGNRLNNVV VEDDAVAAQA IELLKSRRAG RATFLPLNKL RSGRYLERLH EEGAIGYALD
LIEFDRRYEA AFVQVFGDTV VFRSLELARR QLGRYRMVTM AGELLEKSGA MTGGSLDARR
GGSGFALSEP PELAEMRARL GDLDRLLATL AERLERREQR AHELQSAAEA AQRELVAIEN
RAEQLGREHS TQQARATQLR VFLDSCQVGL EADRQEQADL AARLGPLREQ IVQVREELAK
LEQSDNHHRW QQSQQHLREL ETEVRRWELQ LRHAEADLQK SHLDEQLAQE KRQNLLSRRL
DWEDQKVEFG QREEESRTRL AEFDRVIAEL AAQVAELEER LVDIKRERDR LEAHGRALQQ
RQGQLNLQRE QERLHQGQRA AALAAAQERL DELGPPAEDV PPPPEDLSLE QLQATRLRKQ
RRLEALEPVN MLAIEEYDRT AERQGELSEK LATLQRERSE LLLRIEDCDT LKRSAFMQAF
DAVNTHFQSL FAELSDGDGH LALEDPDNPF AGGLTLVAHP RGKQVRRLEA MSGGEKSLTA
LSFIFALQRY RPSPFYAFDE VDMFLDGANV ERLAKMVRQQ ANSTQFLVVS LRRPMIERAD
RAIGVTLARA GHSQVLGVKL AADAS