ID A0A0A3IXF1_9BACI Unreviewed; 1186 AA.
AC A0A0A3IXF1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=CD32_03205 {ECO:0000313|EMBL:KGR87573.1};
OS Lysinibacillus odysseyi 34hs-1 = NBRC 100172.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1220589 {ECO:0000313|EMBL:KGR87573.1, ECO:0000313|Proteomes:UP000030437};
RN [1] {ECO:0000313|EMBL:KGR87573.1, ECO:0000313|Proteomes:UP000030437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100172 {ECO:0000313|EMBL:KGR87573.1,
RC ECO:0000313|Proteomes:UP000030437};
RA Zhang F., Wang G., Zhang L.;
RT "Draft genome sequence of Lysinibacillus odysseyi NBRC 100172.";
RL Submitted (FEB-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:KGR87573.1}.
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; JPVP01000046; KGR87573.1; -; Genomic_DNA.
DR RefSeq; WP_036151157.1; NZ_JPVP01000046.1.
DR AlphaFoldDB; A0A0A3IXF1; -.
DR STRING; 1220589.CD32_03205; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000030437; 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:UP000030437}.
FT DOMAIN 520..639
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 262..499
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 680..833
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 883..917
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 943..1025
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; 134109 MW; D0AC67781FD484D5 CRC64;
MFLKRLEVMG FKSFAERIGI DFVPGVTAVV GPNGSGKSNV TDAIRWVLGE QSAKSLRGSK
MEDVIFAGSE SRKPLNFAEV TLVLDNTDER IAVPYTEISV TRRVYRSGDS EYLLNNQTCR
LKDITDLFMD SGLGKEAFSI ISQGRVDEVL NSRPDDRRLI FEEAAGVLKY KQRKKKAEHK
LVETDENLHR VLDILHELDN RLEPLQIQAS TAKDYVRMST ELKDFDISLI VHDLHVCAEQ
LGSMQKEFAE LESNELLLAG EISTAEKSLR QVRAELKTLD GQLDTSQEDL VEATAEVERW
DGRKALMHEK RSNAEKHLKQ LEASLQIAME EAKKHRLQET EKRTLFDAKQ QEVSSLKQAI
KQLEQALTRS VTEIEEEIET SKNKYIDLLN EEATVKNELK HIDQQLQQQQ ETAERITDRS
AGMQKELEHT MAEKEIVSKQ LKKIQEELKE KLNLYTDMQH SLKQVSVQLD EKQNLLYKAY
QYQQQLKSRR ETLAELEADF SGFFHGVKEV LLARDKGELA GIEGAVAELL QVTGEYSQAI
ETALGAASQH IVTQNEQHAQ QAISWLKKRR AGRATFLPKS VMKSRRLGEN QISAVSSHPS
FVDMAYNLVT FEESNRSIIE NLLGNVLVAA SLDGASQIAR MLGFKYRVVT LDGDIVNAGG
SLTGGSVKQQ TSLFTRKAEL DDLSVKMGEM EQSIQSAERT VAIEKEKVTA LRDELEEVRL
LTEELRTQEQ QQKSALLELD MQEKNLRTSV TLATSEQTSM STRHETLAEQ KEQAEKRLQE
LSTELAELNE LVEQLTIAKA QGDTQKDVLR DQIGEKRSQL AVAQEQLSQL QLTIADVAVG
LSKSNESIEK ISQEIEWFQS DAGLNGPSME EIERSIVEWS IKRQTLLDII AEKREQKEAM
QAKLATIEED MKEKQRMHKG YMEAINTLSI KRSRLQYDQT NLLTQLEENY ELTVEAAAEL
AEEIEDVEQV RRKVKLLKQS IEELGPVNLA AIEEFERVQE RHAFLTEQRN DLLEAKETLH
EAIKEMDGEM STRFHDTFTN VRAQFKNVFR ELFGGGQADL VLIDPENLLE TGIEIVAQPP
GKKLQSLSLL SGGERALTAI ALLFAILNTR PVPFCILDEV EAALDESNVI RYSQYLKKFS
KDTQFIVITH RKGTMEGADV LYGITMQESG VSKLVSVKLE EDVPVG
//
