ID A0A1H7YPL0_9BACI Unreviewed; 1188 AA.
AC A0A1H7YPL0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN05192533_10355 {ECO:0000313|EMBL:SEM47129.1};
OS Mesobacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=930146 {ECO:0000313|EMBL:SEM47129.1, ECO:0000313|Proteomes:UP000198553};
RN [1] {ECO:0000313|Proteomes:UP000198553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48,IBRC-M 10115,DSM 25386,CECT 8001
RC {ECO:0000313|Proteomes:UP000198553};
RA Varghese N., Submissions S.;
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}.
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DR EMBL; FOBW01000003; SEM47129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7YPL0; -.
DR STRING; 930146.SAMN05192533_10355; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000198553; 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:UP000198553}.
FT DOMAIN 519..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 255..324
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 420..499
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 673..861
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 897..938
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; 135182 MW; 13A0CA0276A21A11 CRC64;
MFLKRLDVVG FKSFAERIGV EFVPGVTAVV GPNGSGKSNI TDAIRWVLGE QSAKSLRGVK
MEDIIFAGSD TRKALNFAEV TLTLDNEDQS LPIDYNEVSV TRRVYRSGES EFLINKQNCR
LKDIVELFMD SGLGREAFSI ISQGKVEEIL NSKPEDRRTI FEEAAGVLKY KTRKKKAETK
LFETQENLNR VADILYELEG QVEPLKIQAS MAKDYLEKKD ELEKIEVALT AFEIEELHGR
WEQLSEELKQ HKEGEMQMAA TLQKKEASIE KLRDELTAVD ESISSLQNVL LHASEDLEKL
EGRKEVLKER KKNAAQNKGQ LERTITEIST RIGQLETTKE TQKSAVDILS LEAEKLHKDL
SDRQQQLKLY SEDIELKIES LKSDYIEVLN QQAGAKNELT YIEQQLAQQA VRSTKVGGEN
DRFLQLREEI NQKKAKTKDE LNQVQQALEL EVQKYLQVQR ELEGMRNHLD NQEKTLYQAY
QYVQQAKSKK EMLEDMEEEY TGFFQGVKEV LKARGTKLQG IEGAVAELIK VPKAYELALE
TALGGAMQHI VVANEENGRA AIQYLKRHSY GRATFLPLSV IKGKTIATHL IQAIEGHPSY
VGTAVSLIEF NDKYREVIHN LLGNMVVAKD LKGANELARM LQYRSRIVTL DGDVVNPGGS
MSGGAAKKNA SSLLSRKGEL EELKLKLSEM EEKTNQLEAK FKTSKKELQT RTTHFEDLRK
IGEDLRLKEQ SLKGELREIE IEERNINERL AVYDSEQSQF NEERVRLTHR EAELVKQNAQ
LKDNLKELDR QIAELTNRKN INLTSKETLI SEISELKVAL AAKNEQFQFA KEKLESATLE
LEEQTNRLEA ITDDLALLSS EMTNSSSGEN QLEDAARKKL EDKNNTLELI STRREERLNR
QAQLEDLELE TKELKRQYKG LNEVVKDEEI KLNRLDVELD TRLAHLREEY LLSFEAAKEQ
YPLMISADEA RTKVKLIKLA IEELGTVNLG AIEEYERVSE RYEFLNEQRS DLQEAKDTLY
QVIGEMDTEM KKRFEETFVA IRSHFEGTFQ ALFGGGRADI RLTQPDDLLN TGVDIVAQPP
GKKLQNLGLL SGGERSLTAI ALLFSILKVR PVPFCILDEV EAALDEANVF RFSQYLKSYS
SETQFIVITH RKGTMEEADV LYGVTMQESG VSKLVSVKLE ETNKLVKS
//