ID A0A1S2LCU3_9BACI Unreviewed; 1188 AA.
AC A0A1S2LCU3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=BKP35_15420 {ECO:0000313|EMBL:OIJ09873.1};
OS Anaerobacillus arseniciselenatis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=85682 {ECO:0000313|EMBL:OIJ09873.1, ECO:0000313|Proteomes:UP000180098};
RN [1] {ECO:0000313|EMBL:OIJ09873.1, ECO:0000313|Proteomes:UP000180098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15340 {ECO:0000313|EMBL:OIJ09873.1,
RC ECO:0000313|Proteomes:UP000180098};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-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:OIJ09873.1}.
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DR EMBL; MLQQ01000042; OIJ09873.1; -; Genomic_DNA.
DR RefSeq; WP_071314260.1; NZ_MLQQ01000042.1.
DR AlphaFoldDB; A0A1S2LCU3; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000180098; 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; 1.20.1060.20; -; 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:UP000180098}.
FT DOMAIN 519..638
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..475
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 673..924
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; 137042 MW; 94F453E69F8B860F CRC64;
MFLKRLDIVG FKSFAERTSI DFVPGVTAVV GPNGSGKSNI SDGIRWVLGE QSAKSLRGAK
MEDIIFAGSD TRKPLNFAEL TLTLNNEDHH LAIDYSEVSV TRRVYRSGES EYYINKQSCR
LKDIHELFMD SGLGREAYSI IGQGKIEEIL SSKSEERRVI FEEAAGVLKY KTRKLKAERK
LAETQENLYR VEDIIHELEG QVEPLKIQAS MAKDYLEKKD ELKKVEVGLL VYEIEQLHNQ
WQQQKQKVEQ LSYEQVEISS QIQVEEVKVD DFREKIQAID ESINDLQDVL LRTIEQLEKN
EGQKEVLKER KKNYDQTKED LVEKINNFKA KKVTLEESVK LENEKLIQYK DQLNSTSKQL
SEELKVLASL EEDIETDLER MKADYIEVLN EQASIRNEIR YLQEQLEQRK QKSFYLDNNN
SALLEQRDNL LKNEKLLKEK VLKKQQSINE HALKLGNTNK QLESLTEKFE QMEVQLFEAV
GFVQKIRSRK DVLEEMQADF SGFFQGVKEV LKARGEKLKG IEGAIAELIN VPKNVELAIE
TALGGAMQHV VVGTEENGRQ AIQFLKNHRF GRATFLPLSV IKARDFSPYD RQKLQNHPAF
IGVAVDLINF EEKYRSVISN LLGHVIVAKD LVGANELAKL LHYKNRIVTV EGDVVNPGGS
MSGGSIKQKG SQLLGRQREL DELITKLAQV EKQTELMENK VNELRVERQT KEVLLESLRK
EGEQLRTEEH ELKANLREYE IEVNNLNERL SLYDKEKANF DHEVIEIEKK IALLNENLVK
TEQLKEQLDH QVKTLTEKKK TQQTSKQSLN EFITELKVKV AKEEEQYRNQ KERVITLEKE
QSMLERELKE TEEGYWLLER EMNNNTNGEE SLDEMIEKKR YEKDLTFKFI QERRQERIDI
QNAHDDLERE LKEKKRNQKQ LADYLHTEEV RVTRLDVELE NRLKKLSTDY EISFEAAKAK
YPLPDDAKAS KERVKLIKLA IDELGTVNLG AIDEYTRVSE RFSFLTEQKG DLQEAKETLF
QVIKEMDLEM STRFEATFLQ IKSQFQNVFK ELFGGGQADL QLNHPDNILE TGVDIVAQPP
GKKLQHLALL SGGERALTAI ALLFAILKVR PVPFCVLDEV EAALDEANVS RFANYLKDFS
KETQFIVVTH RKGTMEEADV LYGVTMQESG VSKLVSVRLE ETSELITT
//
