ID A0A1T4NTY3_9FIRM Unreviewed; 1187 AA.
AC A0A1T4NTY3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN02745885_01025 {ECO:0000313|EMBL:SJZ82729.1};
OS Carboxydocella sporoproducens DSM 16521.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVI. Incertae Sedis; Carboxydocella.
OX NCBI_TaxID=1121270 {ECO:0000313|EMBL:SJZ82729.1, ECO:0000313|Proteomes:UP000189933};
RN [1] {ECO:0000313|Proteomes:UP000189933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16521 {ECO:0000313|Proteomes:UP000189933};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) 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 ---------------------------------------------------------------------------
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; FUXM01000008; SJZ82729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4NTY3; -.
DR Proteomes; UP000189933; 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; 1.10.287.1490; -; 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 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:UP000189933}.
FT DOMAIN 525..644
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 234..516
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 676..944
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 973..1021
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 1187 AA; 135657 MW; 860D9535EA94708A CRC64;
MLLKRLEIQG FKSFADRVEL AFNSGLTVIV GPNGSGKSNI ADAIRWVLGE QSVKNLRGSR
LEDVIFSGSV KRKPVGMAEV SLTLDNSNGR FPLEFNEITV TRRVYRNGES EFLINKTPCR
LKDIHELFLD TGLGRDAYSI IGQGRVEEIL NARPEDRRSI IEEAAGIVRY RMRKLEAEKK
LQETEVDLVR VEDIISELEG QLEPLARQAE VAEKYLAYQR EEQELEIGCL VRQGQQVREK
LAELQCQVQE LETAREEAAA ALARVEASRQ KFQRELEPLE AELQAIQDKY TSLLSEGEHT
QGQLQVLSTQ KQGRREQATL LRRQLEEIET ELADSGETAA ADALLVQQLE GKRQQLQSEL
AAVNERAESL QKELDTIRQA LVSQKDSSAQ ALNELTRLEQ QQTAGAIRLA GLREKIEHLR
NQIQEIDRAI TTWQAREKQS QKWQQELERG RQEHESRQVG LAQSRKEMEA ELAQLEEIFN
QKQQQWQLLA SKARVLADMQ QDYEGYQRAV RELLLRRQRG EPACQEICGV VAELLQVPQE
YEIAVEVALG GALQYLVTET DQGAKQAIEY LKGHNLGRAT FLPLNTVTAS TLREEEKATL
LKRPGVIGIA ADLVSYAEKY RPVINNLLGR IIVCQDLDAA LGLARATGFR YRIVTLAGDM
LNPGGSLTGG SYQRRNANLL GRARELEEIN QAAKQVNGER EELRKQIEKI RSSLRENQKQ
KEELETRTAE LRLKLVEAQR DWQEARSRCQ ELEEQREQLL QNLESCQREY TQVERELDSL
ARKAAELETV RQETGNAIEA ENIRLAEQEK ALQNLMARQT ELKVELAQVE QQLTGLKTID
VRQRLERRRR LQQLEQIQRD LAVLEQEGEA LEQRKNELAE HWAKLQQETE RVREKLLELR
QKRQTMQIEE RKLLELWQSS QERLQELERT AHQLELKRTR QEAEWENITQ RLWDDFGMVF
NQEQVIAYQG LDLKQAMRRI KELKALMAEL GQVNIGAIEE YQRIQERYTF LQNQAQDLKE
AKAALYDVIA EMEAIMAQRF AETFAQVAEH FSRVFTELFG GGQARLQLTD PENLLTTGVD
IIAQPPGKKT QQLSLLSGGE KALTAISLLF AILEVRPSPF VVLDEIEAAL DEANVARFAE
YVKNFSDRVQ FLAVSHRKGT MEAADILYGV TMDDSGSSKV LALEMTR
//
