ID E5WD39_9BACI Unreviewed; 1188 AA.
AC E5WD39;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=HMPREF1013_00363 {ECO:0000313|EMBL:EFV79447.1};
OS Bacillus sp. 2_A_57_CT2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV79447.1, ECO:0000313|Proteomes:UP000003283};
RN [1] {ECO:0000313|EMBL:EFV79447.1, ECO:0000313|Proteomes:UP000003283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV79447.1,
RC ECO:0000313|Proteomes:UP000003283};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL Submitted (DEC-2010) 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:EFV79447.1}.
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DR EMBL; ACWD01000004; EFV79447.1; -; Genomic_DNA.
DR RefSeq; WP_009330797.1; NZ_GL635750.1.
DR AlphaFoldDB; E5WD39; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_9; -.
DR Proteomes; UP000003283; 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:UP000003283}.
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..373
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 420..475
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 680..728
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 764..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; 135893 MW; A50B850E4F80E369 CRC64;
MFLKRLDVIG FKSFAERITV DFVPGVTAVV GPNGSGKSNI TDAIRWVLGE QSAKSLRGAK
MEDVIFAGSD SRRAQNFAEV TLTLDNGDQG LPIEYSEVSV TRRVYRSGDS EYLINKQTCR
LKDIVDLFMD SGLGREAFSI ISQGRVEEIL NSKAEERRTI FEEAAGVLKY KTRKKKAEGK
LSETQDNLNR VNDILHELES QVEPLKIQAS IAKDYLQQKE ELEKIEVALT VYEIEDLHSK
WEQLSRQLER HTEDEMKLSA VIQNKEAKME ELKDHIAAID ESVNDLQDVL LHASEELEKL
EGRKEVLKER KKNASQNKDQ LHRNMEELSS KITELKEQEE KQSALKGKIK EEAVKLQKAL
KEKQEQLKLF SENTEEKIES LKSDYIEVLN SQAASRNELQ NIDQQLSQQG QRSSKLEMDN
EKYIADRKKN EEKKQKIQSE LESLQKEIES QVHVFRTEDR KLESLKNNYQ KQEKTLYQAY
QYLQQAKSRQ EMLEEMEEDF SGFFQGVKEI LKARGSKLQG IEGAVAELIQ VPKEYETAIE
TALGGAMQHI IVQNEQDGRS AIQFLKKNSY GRATFLPLSV VKGKRLNTGQ LQSVQGHPAF
IGEAATLIRF EGRHQSAIEN LLGNVVIARD LKGANELAKL LQYRVRLVTI DGDVVNPGGS
MTGGALKQKS TSILSRKGEL EELKSRILDM ESKTANLEKQ VKLQKSEIQK QETRIEQLRK
TGEELRLMEQ RVKGELLEVE FEEKSINERL SLYDMDKAQF SEDRERLLTR KSELADLLEQ
QQKQIADLDN EIKALTERKN TQQTSKETLV SEINELKISF ASKSEQLNHA EDKLAALISE
LAANRDKLKT VKEDLELLSS EMTNSSSGEQ HLEEAAQQKL KEKNETLELI ASRRDERLKL
QTSLEDLELE AKELKRQHKG MVEVLKDEEV KQNRLDVELE NRLNHLREEY LLSFEGAKEE
YPLEIEIDEA RKKVKLIKLA MEELGAVNLG AIEEYDRVSE RYEFLLEQKT DLQEAKDTLF
QVIDEMDVEM KRRFEETFEG IRFHFESVFQ SLFGGGRADL RLTQPDDLLN TGVEIVAQPP
GKKLQNLGLL SGGERALTAI ALLFSILKVR PVPFCILDEV EAALDEANVQ RFSQYLKRYS
DVTQFIVITH RKGTMEEADV LYGVTMQESG VSKLVSVRLE ETRELITQ
//
