ID A0A087N5A3_9BACI Unreviewed; 1186 AA.
AC A0A087N5A3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=CH76_00410 {ECO:0000313|EMBL:KFL44306.1};
OS Lysinibacillus sp. BF-4.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1473546 {ECO:0000313|EMBL:KFL44306.1, ECO:0000313|Proteomes:UP000029097};
RN [1] {ECO:0000313|EMBL:KFL44306.1, ECO:0000313|Proteomes:UP000029097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BF-4 {ECO:0000313|EMBL:KFL44306.1,
RC ECO:0000313|Proteomes:UP000029097};
RA Antwerpen M.H., Georgi E., Zimmermann P., Hoermansdorfer S., Meyer H.,
RA Grass G.;
RT "Genome sequence of strain, BF-4, a Lysinibacillus-like bacillus isolated
RT during an anthrax outbreak in Bavaria.";
RL Submitted (MAR-2014) 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:KFL44306.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPUW01000001; KFL44306.1; -; Genomic_DNA.
DR RefSeq; WP_036141317.1; NZ_JPUW01000001.1.
DR AlphaFoldDB; A0A087N5A3; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000029097; 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; 1.20.5.340; -; 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; 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:UP000029097}.
FT DOMAIN 520..639
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 318..475
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 680..895
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 966..1024
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 1186 AA; 134021 MW; A46EF41BFF440200 CRC64;
MYLKRLDMVG FKSFAKRTSI DFVPGLTAVV GPNGSGKSNV TDAIRWVLGE QSAKSLRGAK
MEDIIFSGSD AHRAVNVAEV TLVLDNSDER VKLPYNEVSV TRRVHRSGES EYLLNNQACR
LKDITDLFMD SGLGKEAFSI ISQGRVDEIL NSRPQDRRAI FEEAAGVLKY KLRKKKAEHK
LFEADENLLR VLDILHELSD RLAPLEQQAS KARDYLQMTA DVRDYDIAVM VADATAQLTA
MQAHQATEQQ YKEQEQHFAK QVAELEVLVQ TLMSERQTLD QQYEATNASL LEASTEVERL
TGYQAVSAEK AQNKAQRLAQ LEAAKAHQAT KINALTEKQQ QERTHFATLQ TQVKEQEQQV
KQYEHVLQRS AKEIDKEIEQ QRNRYIDLMN EQVTVKNDMK HIEQQMARQQ AMTSRVSTQN
DEASEQLRTL QQQFSELTQR NATLHDKLGH LRQQLKQQTQ QVDKQKNAFE KKQAMLYEAY
QHQHRLKARK DTLEELAADF SGFYQGVRAV LQARASNQLQ GIDGAVAELL HVPKQYTQAI
ETALGASSQH IITTDEKAAQ YAIQYLKRKK EGRATFLPRT VIKPRLIQSH ILQEVASHPA
FINTASALVS ADQQYEAIVD NLLGSVIVAQ DLQGATAIAR LAGFRYRVVT LEGDVVNAGG
SLTGGAAQRQ SNVFSRKLEL DDLASKLTQI NAQITTAEAD VQQGKVMLQT QQQQLVQLRE
DIESTQQQAH ASAAQVTALE NDKKHLEARV SVVATERTDA TEQIAQLTAQ YEQATARVTA
LTQELTQIDE QVQSLTNLKE KSELERDTLR AQLDDLRPKL AVSKEKRAQA GEAIAGYELA
LEQAKAELAS IAEDITWFTK EQGEQDSPEV LTQKITAWQT AKQENEQRLQ TLREARATNR
VTLQDKEVTL QQLRMQHQGY VEQLHDIALK IERAHSRITY IEEQLWEQYE WDLRSQQDVP
KLTIDIEQAR RRVKLLKQSI EELGTVNVDA IAEYEQVMER YTFLQEQRND LVEAQQTLNE
AICEMDSEMT VRFKTTFEEI RTHFHSAFRE LFGGGNADLV LIDPTNLLET GIEIVAQPPG
KKLQSLSLLS GGERALVAIA LLFAILKTRP VPFCVLDEVE AALDEANVTR YAEYLRKLSG
DTQFIVITHR KGTMEGADVL YGITMQESGV SKLVSVKLEQ DEEERQ
//
