ID M2Q1K4_9FIRM Unreviewed; 979 AA.
AC M2Q1K4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=HMPREF9943_01559 {ECO:0000313|EMBL:EMD16156.1};
OS Eggerthia catenaformis OT 569 = DSM 20559.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Eggerthia.
OX NCBI_TaxID=999415 {ECO:0000313|EMBL:EMD16156.1, ECO:0000313|Proteomes:UP000011758};
RN [1] {ECO:0000313|EMBL:EMD16156.1, ECO:0000313|Proteomes:UP000011758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT 569 {ECO:0000313|EMBL:EMD16156.1,
RC ECO:0000313|Proteomes:UP000011758};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Mathney J., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lactobacillus catenaformis F0143.";
RL Submitted (FEB-2013) 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:EMD16156.1}.
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DR EMBL; AGEJ01000024; EMD16156.1; -; Genomic_DNA.
DR RefSeq; WP_004803778.1; NZ_KB446649.1.
DR AlphaFoldDB; M2Q1K4; -.
DR STRING; 999415.HMPREF9943_01559; -.
DR PATRIC; fig|999415.3.peg.1586; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000011758; 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; 6.10.140.1720; -; 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.
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:UP000011758}.
FT DOMAIN 419..538
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 228..255
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 332..390
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 576..688
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 979 AA; 111374 MW; F45BA7CE873C2C85 CRC64;
MYLKRVELQG FKSFADKSFI EFMPGVIGIV GPNGCGKSNI TDAIRWVLGE KSAKAMRGDT
MTDVIFSGSE DRKPLNIAEV TLVFDNEDHY LDYDSHEVEI TRRIYRDGSE AQYFINRQSV
RLKDITTLIM DTGLGRDSLS IISQNSINEF VASKPEDRRG MFEEAAGVAK YKARKKESVS
KLARTTENLE RVEDITGELE RQLNPLKRQK EKAEKYLQLS GELQEIEVTV LVKEIEKLNE
KLRILNQELT ESYAHATELE GNIILNENKN TAIQEKMYAL DSEINELQGK LLATMNRVNE
LETQKVEIDA NRKHILENQN EDNLALRIAS MKETLQDALS EYNDRVQRYQ QVKKEKEELE
NKQKEALLKE NLLREEAETL NLKIHAERNE SLRLKELLDS KSNYPYGVRS VLQAKETLSG
IKGTIGDLIS ARENYETALH ISLGAASNHI VTRNQEDAKR AIAYLKRNQA GRATFLPLDV
IKGRTIRGDL ALIARESQGY LGVMSDFVEY DHSLDQIVSN LLGSIIVADH IDHAVKIARN
TSYRLKVVTL SGDIVNVGGS LTGGNYKNKN DGFASKKELE RLNEKLTDHE KELHHKKLEL
SKQENMTREL RQMFMQKQMS FAQLEIVVTN KRNDLQLAKS DYEALTNKSV ELEEIADGSK
SNELLEILNK AKKERDQLKE QIQGKRELRM SYVNENDEIA KTLREERSHL KIIEEAITNN
KINKTKYETE IQNALNRLND SYQLTYEHAL EFVNEGLDTE DAKEKVRDLR IKIAGLGHIN
LDAIDQYTEI SQRYESLNKN RIELIEAKDS LLKAINDMDH IMIDRFTKTF EAVNVEFNRV
FRYLFGGGHA SLHYVDPQDI LETGIEIEAQ PPGKSAKLHS FSGGENALIA LSCLFAIMSV
RPVPLCILDE VEAALDPANV ERFAKYLKEY SDKTQFIVVT HREGTMAECD LLYGATMQQK
GVTKLVSVKL DDATALADA
//
