ID A0A1U7M337_TISCR Unreviewed; 1192 AA.
AC A0A1U7M337;
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_5 {ECO:0000313|EMBL:OLS01734.1};
GN Synonyms=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=TICRE_23340 {ECO:0000313|EMBL:OLS01734.1};
OS Tissierella creatinophila DSM 6911.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tissierellaceae;
OC Tissierella.
OX NCBI_TaxID=1123403 {ECO:0000313|EMBL:OLS01734.1, ECO:0000313|Proteomes:UP000186112};
RN [1] {ECO:0000313|EMBL:OLS01734.1, ECO:0000313|Proteomes:UP000186112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6911 {ECO:0000313|EMBL:OLS01734.1,
RC ECO:0000313|Proteomes:UP000186112};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Tissierella creatinophila DSM 6911.";
RL Submitted (FEB-2016) 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:OLS01734.1}.
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DR EMBL; LTDM01000064; OLS01734.1; -; Genomic_DNA.
DR RefSeq; WP_075728244.1; NZ_LTDM01000064.1.
DR AlphaFoldDB; A0A1U7M337; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000186112; 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 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; 2.
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:UP000186112}.
FT DOMAIN 525..642
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..194
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 241..303
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 381..485
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 683..738
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 823..853
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 914..1032
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 1192 AA; 138805 MW; 22EC93689512C710 CRC64;
MYLKKIHIQG FKSFADKTEI KFKNDITAIV GPNGSGKSNI SDAIRWVLGE QSIKSLRGSN
MVDVIFAGTN KRRALSFAEV TIFFDNKDGI IPLEYNEVAV TRRMFRSGES EYYINKNSCR
LKDIRSLFMD TGIGKDGYSV IGQGKIDEIL SNKPEDRRNI FEEAAGIIKY KTKKEEAERK
LKNTEENLIR INDLIYEISA QYKRLEKDSK KATEFINIFN ELKDLETNIY IKDIKVIDDK
KALIIKDKTQ VEKEIEEKEK EKLKKQNIFD GLKENMDNRE KEIELLRKKR EDIIRLKEES
KNKVLLLLEK ENFCKKDLSR ISEELKDMDD EDIILNKELI LISEHIDLSS SEHNKLISQY
EIKEKQFNYI DKKSIDTEKY IDDKKNEISL LYEKIADKKG ELNNIDSLSL NSDKKILELK
DEEKKLYEKI KKISENIQKL NDDKKTIELN QERLFKDKEI YGLENNKIKE KIDENFQKIK
ELEMQIERIS SGYKLYKTME NSYEGYYKSV KNLLKALKDN NLENKGFHGI VADLLSVNEK
YEIAINISLG GNLQNIVVDN EKNAKSMISY LKTNKLGRVT FLPIDTIKGN ELAIDMENVK
KQGVLGLAHR LIKYEKKYED IFKSLLGRTI VIDNIDNAIK FAKKTNNSYR IVTLEGELLN
PGGSLSGGSY KDNINIINRK VKIENMEKIL SNLKVDLSNL RTENLVFQKE FKLIEEKIDI
LKNNIEIDNI NLRNIENDKK TFKNEEEFFG KNLEKTRCQI KELINSSRAN LEKTLQNKII
LKIDIDRLEE LKENVKINID SLTICKENRE KAYKDISEIK LSIKLIESKL LNYKNEVKNL
KQKKINNKLL KEEKLKEIIV VKKDLEKIIL DKQVSETSMQ ESFKEEVNLK NDIEIKVEDK
DKYMNNFYKE QTIIKTLIEN ISTLERNKND KDLKLSRLEM ERENITSKLL ADYKLNIEEA
FLLERSIDNI KESRKRIKLL KEKIKHLGNV NLGALEEYRE VKQRLEFMET QHNDLIESKE
SLKDIIRDME KEMKLNFLNS FEEIKNNFSK VFSELFNGGS AILELENTED DILKSGIEIK
VKPPGKVFQS LSLLSGGEKS LVAVALLFAI LKVKPSPFCI LDEIDAALDD ANISRYTSYL
KKINDDTQFI LITHRKTSME IANVLYGVTM EEKGISRIIS MKLKENKNEL VS
//
