ID E3CGG3_STRPA Unreviewed; 1178 AA.
AC E3CGG3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-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:EFQ54397.1};
GN ORFNames=HMPREF9626_0613 {ECO:0000313|EMBL:EFQ54397.1};
OS Streptococcus parasanguinis F0405.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=905067 {ECO:0000313|EMBL:EFQ54397.1, ECO:0000313|Proteomes:UP000003812};
RN [1] {ECO:0000313|EMBL:EFQ54397.1, ECO:0000313|Proteomes:UP000003812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0405 {ECO:0000313|EMBL:EFQ54397.1,
RC ECO:0000313|Proteomes:UP000003812};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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:EFQ54397.1}.
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DR EMBL; AEKM01000016; EFQ54397.1; -; Genomic_DNA.
DR RefSeq; WP_003005473.1; NZ_AEKM01000016.1.
DR AlphaFoldDB; E3CGG3; -.
DR Proteomes; UP000003812; 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; 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|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..208
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 241..373
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 438..482
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 677..924
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 1178 AA; 134018 MW; E46983CB0A6E1904 CRC64;
MYLKEIEIQG FKSFADKTKV VFDKGVTAVV GPNGSGKSNI TESLRWALGE SSVKSLRGGK
MPDVIFAGTE SRKPLNYACV TVVLDNQDGF IQQAGKEIRV ERHIYRSGDS EYKIDGKKVR
LRDVHDLFMD TGLGRDSFSI ISQGRVEEIF NSKPEERRAI FEEAAGVLKF KTRRKETETK
LNQTQENLDR LEDILYELEG QIQPLEKQAT VARRFLELDQ ERQVLLLDVL VAQVDLTKDL
YEKADQEEKA IQEQLASYYQ RRQVLEEDNV RIKKARHQLD ESLAEDQASL LEVTRLISDL
EKQIEVAKLQ SSQAAHSRRE NLERLDAVVA RLEEAKQELA QKQETLAALQ QRLTENRQQQ
EELEKELANY EEDPEQVIEH LREQYVALLQ TEAEKSNERT AIESRIQALL QESSHRQEDL
VKAQTNFEAA KEKEIRQLEE LDQAQAMVKR LLAEYQNQLV KVEQAKAAYQ EAQTAMFDLM
DESKNKRARI NSLEAIQKNH SNFYAGVKSV LQEAERLGGI CGAVSENLSF SKDYQTALEI
ALGASSQQII VEDEKAATRA IDFLKRNRLG RATFLPLTTI KARQLSHRNL ELIQTSAGFL
GIASDLVTYE HRFEQIFQNL LGVTAIFDTT EHAREAARKV NYQVRMVTLD GTELRTGGSY
AGGANRSQNT VFVKPELDSL KQEMQALDAR LREAEQEVET KDNLLKQAQE YLASIQSQGE
QARLEQQRAQ LAYQQSQEQL KEIQELLEAL KSELATDATQ SLQEEQEALT EQLVEIELQK
ENLNRDIETM KSDKDVLQQK VQNLQEQLAD LRLQQTECKS QQSYEQTDAR RLEETISQLE
VEEHQLQLLI EQGEAQVQTV DVEQLANQLA QAQAKKTDLE QGVIRKRFEL DDLEGQAEDV
AEQMEQARKK NEEWIRQQAK AEATREKHAD RLNKLLTQIT DEFMQSFDQA KEQAKPVENL
AAAENQLKSI EKDIKALGPV NVDAIEQYDE VKGRFDFLSS QREDVLAAKN MLLSTINDMN
DEVKERFKST FEAIRESFKV TFRQMFGGGS ADLILTEPDL LTAGVEISVQ PPGKKIQSLN
LMSGGEKALS ALALLFSIIR VKTIPFVILD EVEAALDEAN VKRFGDYLNR FDKESQFIVV
THRKGTMSAA DSIYGVTMQE SGVSKIVSVK LKDLENEE
//
