ID A0A1C1A0D2_9BACL Unreviewed; 1191 AA.
AC A0A1C1A0D2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=A8709_19935 {ECO:0000313|EMBL:OCT13846.1};
OS Paenibacillus pectinilyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=512399 {ECO:0000313|EMBL:OCT13846.1, ECO:0000313|Proteomes:UP000093309};
RN [1] {ECO:0000313|Proteomes:UP000093309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC13222 {ECO:0000313|Proteomes:UP000093309};
RA Zhang J., Zhang X.;
RT "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL Submitted (MAY-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:OCT13846.1}.
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; LYPC01000022; OCT13846.1; -; Genomic_DNA.
DR RefSeq; WP_065853944.1; NZ_LYPC01000022.1.
DR AlphaFoldDB; A0A1C1A0D2; -.
DR STRING; 512399.A8709_19935; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000093309; 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:UP000093309}.
FT DOMAIN 521..640
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 742..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 269..296
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 386..497
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 892..947
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 748..771
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 1191 AA; 135329 MW; 671B196B6D5B103C CRC64;
MFLKRIELSG FKSFADRTEL EFVRGITAVV GPNGSGKSNI SDGIRWVLGE QSAKSLRGGK
MEDVIFAGSD ARRAVNYGEV SLTLDNTSQS LPLDFNEVTV TRRVHRNGDS EYLINKQPCR
LKDITELFMD TGIGKEAYSI IGQGRIEEIL STKSEDRRGI FEEASGIVKY KSRKREAEKK
LNDTEQNLLR IHDLVSELED QVEPLREQSE KAIRFKELKE TLKSSEISMY VHQIDQIYIA
WNDATQLLEK LTKEQTELST IVNQHDAHLE KHRWETRRLE EELETLQESL LGLSEEFEKC
EGHGEVLKER KKNYVTNHQQ LSTTIAMQEQ RKLDKEADLS EQRDKIISIG AQLFEFQAKL
TAEEQRLQGV SGGISSSPED QLKGELLETL NRMAQSRNEI RYAEQQIESI GRRLERLDEE
RQKWADQRES ITRRKQELSA KLEETVADIE KARLQYVQLT QALKSKQGLL DEAQAMVRKW
EQKLDALISR RDTMKEMAND YDGFQQGVKE VLKAKTRKDL RGIRGAVAEL VKVPANVEIA
IETALGGALQ NIIVETEADG REAIAFLKRR QMGRATFLPM NVIRGRSISD HESHTLKASK
GFVGIAVDLV SFDATYTNIF SSLLGNVVVA ESLEDANHIA AKAQYRYRVV TLEGDVVNPG
GSMTGGSLQK KSTNLLGRQR QIEELDAEIA SSEGQLSGLR SQSSSLKREI TDEMLAVEQL
RQLGEQQRIT EQQIRAELNP LESESRTVEA QLKIDSQDRG ALQEERTEFG RKKVESEAAL
AQLQEEEASL QQAIRDAESS RKASESEKEE LQSQLTDLKV KVASTSQEKQ SLQDQQRRLQ
QDLSDVEREI ELNRGLLSQL DRDMATLEQE TVQQIELLND LKLRKQQCSE SIDFKRAERT
EWLQKLEQGE NETRTQRVQL KQVEENLHQT EVRVTRLDVE LENLLKKLAE EYELGYELAK
LRYPVPEDIQ GTQQKVREFK REIASLGDVN LGAIEEYARV SERFEFLSSQ KDDLIEAKTT
LYQVIREMDI EMSKRFKTTF DAIRSHFGVV FAKLFGGGRA DLILSEPENM LDTGIEIVAQ
PPGKKLQNLQ LLSGGERALT AIALLFSIIR VKPVPFCVLD EVEAALDEAN VSRFAEYLRE
FSEMTQFIVV THRKGTMEEA DVLYGVTMQE GGVSKLVSVR LEDEEATMTA S
//