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Database: UniProt
Entry: A0A0P8YAF0_9CLOT
LinkDB: A0A0P8YAF0_9CLOT
Original site: A0A0P8YAF0_9CLOT 
ID   A0A0P8YAF0_9CLOT        Unreviewed;      1188 AA.
AC   A0A0P8YAF0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc_3 {ECO:0000313|EMBL:KPU43938.1};
GN   Synonyms=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=OXPF_21030 {ECO:0000313|EMBL:KPU43938.1};
OS   Oxobacter pfennigii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Oxobacter.
OX   NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU43938.1, ECO:0000313|Proteomes:UP000050326};
RN   [1] {ECO:0000313|EMBL:KPU43938.1, ECO:0000313|Proteomes:UP000050326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU43938.1,
RC   ECO:0000313|Proteomes:UP000050326};
RA   Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT   "Genome sequence of Oxobacter pfennigii DSM 3222.";
RL   Submitted (SEP-2015) 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:KPU43938.1}.
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DR   EMBL; LKET01000032; KPU43938.1; -; Genomic_DNA.
DR   RefSeq; WP_054875150.1; NZ_LKET01000032.1.
DR   AlphaFoldDB; A0A0P8YAF0; -.
DR   STRING; 36849.OXPF_21030; -.
DR   PATRIC; fig|36849.3.peg.2221; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000050326; 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; 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:UP000050326}.
FT   DOMAIN          524..642
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..366
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          414..464
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          677..869
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          908..949
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          999..1033
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   1188 AA;  135735 MW;  57DBB1CFCAFBE244 CRC64;
     MYLKKIEVKG FKSFADRIEL ELDKGITGVV GPNGSGKSNI SDAVRWVLGE QSAKSLRGGK
     MEDVIFAGTD IRKPLGYAEV AITIDNQDSM LPIDYSEVII ARRMYRSGES EYSINKVNCR
     LKDITELFMD TGVGREGYSI VGQGRIDEIL SAKPEDRREI FEEAAGIVKY KTRKQESEKK
     LDATEQNIVR LDDIINELNS QLEPLMIQSE NARKFLDTRE KLKVLELNIH VINIEKIKEK
     LTGVNDLMSG LEAEFKDKTS RISEIDNEYL SVKGIIQKMD ESISRMQQEI HNIDNEIERL
     QGEGNVLNEK TSNIEKNIIR IDEEIKKEAC EIDKMKKNFE EIDLSLTQST EVLKEQMELL
     EEKNNRFVTL NSSIAEKNDY IENMKSEVIE ILNMIADKRS SVNSYITFKS NIEKRKGQAV
     IESQEKEKDK LRLENDYAKC NEELKTYKKN LEEEKDIIEK IEKGRADTFN EKKKIDERIY
     DINGKLQSMQ ARHRVLHEME EDFEGYNKSV KEIMKLRKNK KYSEGICGVV ADLIHVPEKY
     EVAAEIALGP ALQNIVTENE MWAKDCIEYL KENKYGRATF LPLTTIKGRD ISSNESLVKI
     MPGFLGFANE LITYEKKYFN IIKSLLGRVI VADNMDNAIG IAKKISYSMK VVTLEGEVIN
     SGGSFTGGSL NQRTGNILSR KRELEELERN IKKLNESLYV ANKKKVEIDS TLNELDINAK
     ERTEKKHSLE MMLTTLDNRL TQLKSEIQRA AADIASLNTE IIQLDMENDE VSKKITLESA
     ELREYEARSF NLNTDIQNEQ SGIKDFLNDK DELINEITSI KVKAAQCEQE IGVYKDRIEE
     INNNINEYNR EVQNKIAEKE NSAKEIENIA LLIKENGDKI SSYIKKGEEL KVILTDETEK
     RAKNITSLEE FEAKKKKGTE EIASIQSEIH KADLQKSKLD MELESIQNKI WDDYEISYAA
     AVKYRIEITN ISQAVKEINT LKEEIRGLGT VNINAIEEYK KVKERYGFLT EQRKDLEEAK
     DSLKKVIVEM TDKMRTQFIK NFEIIKENFT VTFKQLFGGG RAELVIVNPE NMLESGIDII
     AQPPGKKLQN LTLLSGGEKA LTAIALLFGI LRMKPSPFCI LDEIDAALDD VNVARYARFL
     KEFSEQTQFI TVTHRKGSME AADVLYGVTM EEKGVSRIVS IKLSEKAS
//
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