ID A0A265NFV0_9BACI Unreviewed; 1188 AA.
AC A0A265NFV0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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 ECO:0000313|EMBL:OZU90349.1};
GN ORFNames=CIL03_04165 {ECO:0000313|EMBL:OZU90349.1};
OS Virgibacillus indicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=2024554 {ECO:0000313|EMBL:OZU90349.1, ECO:0000313|Proteomes:UP000216498};
RN [1] {ECO:0000313|EMBL:OZU90349.1, ECO:0000313|Proteomes:UP000216498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IO3-P2-C2 {ECO:0000313|EMBL:OZU90349.1,
RC ECO:0000313|Proteomes:UP000216498};
RA Xu B., Hu B., Wang J., Zhu Y., Huang L., Du W., Huang Y.;
RT "Virgibacillus indicus sp. nov. and Virgibacillus profoundi sp. nov, two
RT moderately halophilic bacteria isolated from marine sediment by using the
RT Microfluidic Streak Plate.";
RL Submitted (AUG-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 -!- 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:OZU90349.1}.
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DR EMBL; NPMS01000001; OZU90349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A265NFV0; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000216498; 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; 2.
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:UP000216498}.
FT DOMAIN 520..639
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 864..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..289
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 318..380
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 413..475
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 681..841
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 876..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 137851 MW; F384158AA75BF610 CRC64;
MYLKRLESVG FKSFAKRINV EFVPGVTAVV GPNGSGKSNI TDAIRWVLGE QSAKSLRGSR
MEDIIFQGSD SRSALNVAEV TLVLDNHDKE LPLDYEEISV TRRVYRSGDS EFYLNKQSCR
LKDIIDLFMD SGLGREAFSI ISQGKVEEIL SSKAEERRSI FEEAAGVLKY KQRKKKAEYK
LAETQENLNR IEDIIHEIEQ QINPLKEQAE TAEKYIDLKD QLKEKEISYL ITEIETYHEQ
WQTLLDELEK EKMEEIQIKT AIQKKEAGLE DERQKIVQLD EEVEVLQASL LTVTQQLEHY
EGRKQLYNER TRNFTENKEK LKVQKQETEM RIASLQEELK VEKEKLAELQ EIKQKTNKIA
EELEMKLATD EQNIADKIEE LKTIYIENLN VQAAKRNETN SISQQLQQIS GKKERQSQKF
QSLIEHREKL SREYKETQDK YYARQNYCAV QESQMKQLKN ELEQQRKHFQ ESQEKLYKGF
QYIEKLKSKK EMLEEMKEDF QGFFNGVKAV LKAREEKQLQ QIHGAVIELI DIPKKYITAM
ETVLGGQAQH IVVSDDESAR SAISWLKKTN NGRATFLPLK SIQERFITRD VLTEIQKHSG
FVGTASSLVE TDDRFKKCVN HLMGHVVIAE TLKDANEIAG KVKRRYRVVT LDGDVVHPGG
SMSGGAKKRT NQSLFTREKD LQEITEKLDE VQGRAERFEE MVSSLKLQLS HKEKELEQKE
LSITEAQQEL QKVQEAHKEL EMQLASLNNN LSIYDQDKQQ FNQDRGDLQS RQRQLTEDLD
GISQQLQSTQ AEIDSLTRQQ EEFKENQEQM RNELHKNQVS LAEQEERLKS QREKTDSVKK
LISENQLQLE EFTSELDDLI SFNKSDETEE EIDQTIENNK EEKTKITTSI QEKRKQRSER
TKLTQDQERE LKEENKKHQS FIQEIQQKEV KANRLDVELE NRLSRLQTEY TITYEKAKQN
YKKAEEPEQA KSVVQQLKQR IEQLGTVNLG AIDEYDRVKT RYTFLTEQKD DLVEAKQTLF
AVISEMDEEM QKRFDSTFTQ IKQEFAIVFK QLFGGGHAEL KLTDPKNLLD TGVDIIAQPP
GKKLQHLGLL SGGERALTAI SLLFAILRVR PVPFCVLDEV EAALDEANVV RFAKYVKLYS
KQTQFIVITH RKGTMEEADV LYGVTMQESG VSRLVSVRLE DTKELIQS
//
