ID D2MPY8_9FIRM Unreviewed; 977 AA.
AC D2MPY8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
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:EFC05441.1};
GN ORFNames=HMPREF9013_0378 {ECO:0000313|EMBL:EFC05441.1};
OS Bulleidia extructa W1219.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Bulleidia.
OX NCBI_TaxID=679192 {ECO:0000313|EMBL:EFC05441.1, ECO:0000313|Proteomes:UP000005017};
RN [1] {ECO:0000313|Proteomes:UP000005017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1219 {ECO:0000313|Proteomes:UP000005017};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) 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:EFC05441.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADFR01000014; EFC05441.1; -; Genomic_DNA.
DR RefSeq; WP_006627451.1; NZ_ADFR01000014.1.
DR AlphaFoldDB; D2MPY8; -.
DR STRING; 679192.HMPREF9013_0378; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000005017; 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; 1.
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 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; 3.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000005017}.
FT DOMAIN 416..535
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 168..373
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 659..714
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 749..818
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 977 AA; 111646 MW; C6B56ACAB79E3F8D CRC64;
MFLKRVEMQG FKSFADKTVI EFNHPITGIV GPNGCGKSNI TDAIRWVLGE QSAKSMRGDK
MNDVIFAGSA NRRKVNLAEV TLVFDNSDHI LNQQEGEVEV TRRLYRESGE ANYLINHRPV
RLKDIVDLFL DTGLGKDSLS IISQGNVLSF AESKPIERRS IFEEAAGVAK YKKRKLETLS
RLERSEQNLE QNRLVLSELE KQVSPLKRQA KKAELYREKK QRLQKIEISV LVNSIQSLYE
DLEALDQQLF EINTKKTVCQ TDIEVGESQI QVWRKEIHEM DHRVQKLQDE LMNANNSIVA
LEARKSEWEE KSKYILEVGD AKQRQQELQH LYQNAKLEYE DRLARQNSYE QAIQLSQNQL
ASISTELLDY KNELDISSFR YQKMENQLQV LEQLQKNPFN HHAGLKAIVE HQSSLNGIIG
VIGQLIQVQP NYEEAISTAL GGAIHQVLTE NEVAARHAID FLKRNQAGRC TFLPLTVCQA
RYISKEVLTI AQNQDGYLGL ASDYVHIDEK YQAVVAALLQ NVLVVENLEK GNILSSLIHR
QYKIVTLDGE VIHRGGSMTG GRFKQETNLM TIKKEFHAVR ANLEALLAKR ELAQKKYEKG
EADRKKVASI LEENRLSLAS LLPVVEAKKA RMDKYHADLE LLGQHDQKKE EGPSFIFDLN
EAYQMRDEVT KKIQSLRQER YQLGNQLERK EAQLRQKRSE LNDVQQDSHH LEIEKSKQET
KLETNLQRLS SEYQMTYQFA KKKVDVHDFK QEEMEVQQLR QDIEALGNIN MEAPEQYAEV
NERYELLEKH IQEIETSIEQ LLKAVDEMDE VMKKQFEETF IQVNEAFGET FSAIYGGGKA
FLRLQDPDDL LGTGIEIFAQ PPGKTVHNNL LFSGGEKSLI ALSVLFAILK VKPIPLVILD
EVEAALDPAN VSRFAQYLTH YVEKSQFLVV THRPGTMEKA DVLYGVTMQQ QGVSSLLKVN
LVEAIHYGAD DKKGDGE
//
