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Database: UniProt
Entry: A0A0R2MB32_9LACO
LinkDB: A0A0R2MB32_9LACO
Original site: A0A0R2MB32_9LACO 
ID   A0A0R2MB32_9LACO        Unreviewed;      1186 AA.
AC   A0A0R2MB32;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=IV64_GL000539 {ECO:0000313|EMBL:KRO08451.1};
OS   Lactiplantibacillus xiangfangensis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=942150 {ECO:0000313|EMBL:KRO08451.1, ECO:0000313|Proteomes:UP000051783};
RN   [1] {ECO:0000313|EMBL:KRO08451.1, ECO:0000313|Proteomes:UP000051783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26013 {ECO:0000313|EMBL:KRO08451.1,
RC   ECO:0000313|Proteomes:UP000051783};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01894}.
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:KRO08451.1}.
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DR   EMBL; JQCL01000080; KRO08451.1; -; Genomic_DNA.
DR   RefSeq; WP_057707045.1; NZ_JQCL01000080.1.
DR   AlphaFoldDB; A0A0R2MB32; -.
DR   STRING; 942150.IV64_GL000539; -.
DR   PATRIC; fig|942150.3.peg.552; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000051783; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Cell cycle {ECO:0000313|EMBL:KRO08451.1};
KW   Cell division {ECO:0000313|EMBL:KRO08451.1};
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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}.
FT   DOMAIN          519..638
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          300..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          680..749
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;  131900 MW;  BEE6E3860B12C433 CRC64;
     MQLKSLEISG FKSFADKTKI DFQAGMTGIV GPNGSGKSNI IEAIRWVLGE QAVKSLRGTK
     MTDVIFAGSA NRKPLNMAKV TITFDNSDHF LPLDYAEVSI TRKLFRNGDS DYLINNQSCR
     LKDITNLMID TGLGKDSFSV ISQGRVEAVF NAKPEDRRSI IEDVAGVLKY KKDKSTTEAK
     LAETTDYLDR VNDIIAELAQ QKGPLEQQAS LARDYQDQKQ KYDDLDRSRL VKKMTIAHDQ
     LVTVNQKLTG AKTLVAQYQQ QVDAGATKLA TLTAQQAEQR QLKDQLAAKN LELTKTIENT
     QGQQGVDAER RQNQQATQSR LQAELANATD QLASLGEQRS QLTAQLSQQR EQIKKLKATV
     AELTTATSEA GRKQLADQLT ALRNAYVDEK QVQAELNNEA KNLVKQHQQA GNQTDALAQR
     LVTAQANLKR AQTTVDVHNR DQSTLQNQLT QQQTALTQQR EQFKANAVKI DQQQQRWLDA
     AGMMQREKSR LEALQSVQER YTNFYAGVRM VLQHRQQFAG VAGAVSELLT VPSSYTKAVE
     VALGGQLQNI VCDTQQTAKV VVNFLKQNHA GRATFLPVDR IQARQLAVNT EHELQQQPGV
     LGIASELVDC EPQLLAIKRY LLGTTVIVDT LDHAMAISRT RRFRCKLVTV GGETIAASGA
     ITGGATRHDD NGLLQQQQSA EKIAANVDQM QGELITYEKD LADAKKANQD LSSQIETNQQ
     RLSDLKDQLN QVQAQLQAAQ SEQTQLARQV KALDYEQRQR SQADDSYEDQ VTRNEQAKAD
     NDAKLKDYQA QMATVEQQQN DYEAYQKAQS SRLQDQREQL VTLQERCKQT QVQVEQCDQQ
     VQQQTQAQAQ ARASLEEIKT DLASQQMSVQ ERASVLKTAQ ASQAKVLQAR KDCDQRLGDL
     NDTVEELSDQ QVRNQQLAAA ATDDYRRLEL SQTKLTGEVD HATADLAEKY SLTVEAAKSD
     VSDLELPAIN EQLKLLKRGL DEIGTVNLGA IEEFDRVKER YDFLSLQASD LKESKAHLLQ
     TMADLDTTVA TRFKTAFDQV AKQFSTIFVQ MFGGGKAELI LTDPEHLLTS GVDIMAQPPG
     KKFQRLSLLS GGERALTAIT LLFAILAVRP VPFSILDEAE AALDDANVDR FSQYLNDFQT
     GTQFVIITHR KGTMMHADVL YGVTMEESGV SKMVSVSLAD LKNEQN
//
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