ID I0T1F2_STRMT Unreviewed; 1179 AA.
AC I0T1F2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:EID29455.1};
GN ORFNames=HMPREF1048_1130 {ECO:0000313|EMBL:EID29455.1};
OS Streptococcus mitis SK575.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1095736 {ECO:0000313|EMBL:EID29455.1, ECO:0000313|Proteomes:UP000005505};
RN [1] {ECO:0000313|EMBL:EID29455.1, ECO:0000313|Proteomes:UP000005505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK575 {ECO:0000313|EMBL:EID29455.1,
RC ECO:0000313|Proteomes:UP000005505};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2012) 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:EID29455.1}.
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DR EMBL; AICU01000012; EID29455.1; -; Genomic_DNA.
DR RefSeq; WP_000280967.1; NZ_AICU01000012.1.
DR AlphaFoldDB; I0T1F2; -.
DR PATRIC; fig|1095736.3.peg.239; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000005505; 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..465
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 677..859
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 890..973
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 1179 AA; 134062 MW; D837F504FC6D60D1 CRC64;
MYLKEIEIQG FKSFADKTKV VFDQGVTAVV GPNGSGKSNI TESLRWALGE SSVKSLRGGK
MPDVIFAGTE SRKPLNYASV VVTLDNNDGF IKDAGQEIRV ERHIYRSGDS EYKIDGKKVR
LRDIHDLFLD TGLGRDSFSI ISQGKVEEIF NSKPEERRAI FEEAAGVLKY KTRRKETESK
LQQTQDNLDR LEDIIYELDN QIKPLEKQAE NARKFLDLEG QRKAIYLDVL VAQIKENKAE
LDSTEEELAQ VQELLTSYYQ NREKLEEENQ TLKKQRQDLQ AEMAKDQGSL MDLTSLISDL
ERKLALSKLE SEQVAHNQQE AQARLAALED KRKSLSKEKS DKESSLALLE ENLVQNNQKL
NRLEAELLAF SDDPDQMIEL LRERFVALLQ EEADVSNQLT RIENELENSR QLSQKQADQL
QKLKEQLATA KEKASQQKEE LETAKEQVQK LLADYQVCAK EQEEQKSSYQ AQQSQLFDRL
DSLKNKQARA QSLENILRNH SNFYAGVKSV LQEKDHLGGI IGAVSEHLTF DVHYQTALEI
ALGASSQHII VEDEESATKA IDFLKRNRAG RATFLPLTTI KARTISSQNQ DAIAASSGFL
GMADELVTFD TRLEAIFKNL LATTAIFDTV EHARAAARQV RYQVRMVTLD GTELRTGGSY
AGGANRQNNS IFIKPELEQL QKEIAEEEAS LRSEEATLKT LQDEMARLTE SLEAIKSQGE
QARIQEKGLF LAYQQTSQQV EELETLWKLQ EEELDRLSEG DWQADKEKCQ ERLATIASDK
QNLEAEIEEI KSNKNAIQER YQNLQEEVAQ ARLLKTELQG QKRYEVADIE RLGKELDNLD
IEQEEIQRLL QEKVDNLEKV DTELLSQQAE EAKMQKINLQ QGLIRKQFEL DDIEGQLDDI
ASHLDQARQQ NEEWIRKQTR AEAKKEKVSE RLRHLQSQLT DQYQISYTEA LEKSHELENL
NLAEQEVKDL EKAIRSLGPV NLEAIEQYEE VYNRLDFLNS QRDDILSAKN LLLETITEMN
DEVKERFKST FEAIRESFKV TFKQMFGGGQ ADLILTEGDL LTAGVEISVQ PPGKKIQSLN
LMSGGEKALS ALALLFSIIR VKTIPFVILD EVEAALDEAN VKRFGDYLNR FDKDSQFIVV
THRKGTMAAA DSIYGVTMQE SGVSKIVSVK LKDLESIEG
//
