ID A0A1G8DCH3_9RHOO Unreviewed; 1166 AA.
AC A0A1G8DCH3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN05660652_01891 {ECO:0000313|EMBL:SDH55442.1};
OS Propionivibrio dicarboxylicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=83767 {ECO:0000313|EMBL:SDH55442.1, ECO:0000313|Proteomes:UP000198607};
RN [1] {ECO:0000313|EMBL:SDH55442.1, ECO:0000313|Proteomes:UP000198607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5885 {ECO:0000313|EMBL:SDH55442.1,
RC ECO:0000313|Proteomes:UP000198607};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNCY01000006; SDH55442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8DCH3; -.
DR STRING; 83767.SAMN05660652_01891; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000198607; 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; 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; 1.
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|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000198607}.
FT DOMAIN 518..620
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 170..211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 237..341
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 437..464
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 661..716
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 759..800
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 883..938
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 982..1013
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 1166 AA; 132039 MW; D248BCCA924E6400 CRC64;
MRLTKLKLAG FKSFVDPTTI ALPGQLVGVV GPNGCGKSNV MDAVRWVLGE SKASELRGES
MQDVIFNGSG GRKPVSRASV ELVFDNSLGR ISGQWSQYSE LSVKRLLTRS GQSEYYINNL
HVRRKDITDL FLGTGLGPRA YAIIGQGTIS RIIEARPDEL RVFLEEAAGV TKYKERRKET
ENRLSDTREN LTRVEDIRVE LGSQMERLEE QAAVARQFRE YHESLTRKQQ LLWLLRRNEA
QTERERVARE VERAVNELEA QNAALRETEA KLEEARENHF IATDGVQSAQ SENYKASAEV
ARLEAEIRHR RESQSEYESR LTQLQADKQQ WEADVEKYDA DQTRWEELSV LADERAEQGE
MRLAAQQERL PLVEEAYAEV QEAVNTQRGE IARAEQRLQV ELTNRGHAQR SLQILASRRD
RLNQEREALP VPDHAEFEFK QELLAELREK IATAQEDLMS RQRALPGLDQ QRRQVMADVQ
LVQKERAEAH ARRIALEQLQ KRVQGDGKVG EWLRRYHLEK HEPLWKSLHV DAGWEDAVEA
VLRERLNALS ADDVDPAWDK DRPGSKLTLL LPVGGGETKH RHDSLMAKIR CDDARLAAIL
ADWLGDVHAV PSLQAALDRR ETLTGNACCV TPHGDVITRQ SVTLFAADAA EHGLLERQRE
IEELGRIIAE REERVEQAQE RLAEIEATIA DAQNSLQEAR RELDVLQEQA HAIQVETLKL
SQALDRFRER QEQIDASFAD MAAEEEAENE RLFMADEAVE SAREAIRELQ MRLDAISARF
EQAERTLRDE RERVNAAERE WREAQFSQRE CRTKLGEIKN NRDLALKQID RIADELVRCA
ETAEAMQSED LEPQLQAALE RRVACEQALI TARDAQEAAA GALRTLEEQR MKVELSLEPL
RERIGDFRLK EQAAALNVEQ MAAQLEEAQA DEASLSLDLP NARPSALQGA ITTLQRSIEA
LGPVNLAALD ELESARERKG FLDAQSEDLT QAMETLENAI RRIDRETRDL LQATYDTVNK
NFGELFPILF GGGEARLIIT GEEILDAGVQ VMAQPPGKKN STIHLLSGGE KALTAIALVF
AMFRLNPAPF CLLDEVDAPL DDTNTERFCA MVQRMSTNTQ FLFISHNKIA MEMAQQLVGV
TMQESGVSRI VEVDMEEALR MREQIL
//
