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Database: UniProt
Entry: A0A0R1HRN5_9LACO
LinkDB: A0A0R1HRN5_9LACO
Original site: A0A0R1HRN5_9LACO 
ID   A0A0R1HRN5_9LACO        Unreviewed;      1184 AA.
AC   A0A0R1HRN5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=FC96_GL000220 {ECO:0000313|EMBL:KRK49296.1};
OS   Secundilactobacillus kimchicus JCM 15530.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1302272 {ECO:0000313|EMBL:KRK49296.1, ECO:0000313|Proteomes:UP000050911};
RN   [1] {ECO:0000313|EMBL:KRK49296.1, ECO:0000313|Proteomes:UP000050911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15530 {ECO:0000313|EMBL:KRK49296.1,
RC   ECO:0000313|Proteomes:UP000050911};
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: 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:KRK49296.1}.
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DR   EMBL; AZCX01000001; KRK49296.1; -; Genomic_DNA.
DR   RefSeq; WP_056941683.1; NZ_AZCX01000001.1.
DR   AlphaFoldDB; A0A0R1HRN5; -.
DR   STRING; 1302272.FC96_GL000220; -.
DR   PATRIC; fig|1302272.5.peg.217; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000050911; 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; 1.10.287.1490; -; 1.
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; 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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050911}.
FT   DOMAIN          519..640
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          255..373
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          407..475
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          826..923
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          993..1027
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   1184 AA;  132099 MW;  FCE048CE09B7A4FA CRC64;
     MKLKSLEISG FKSFADYTKI EFEDGVTGIV GPNGSGKSNV TEAIKWVLGE QSAKNLRGAK
     MPDVIFAGTS KRRPLNRAMV TMILDNSDHY VESDYTEVSV TRKLFRNGDS RYELNGQECR
     LKDITDLFSD SGIGGNAFSM ISQGRVEAIF NSKPEDRRFI IEEVTGVSKY KSDKEKAKRE
     LEQTAGYLNR VNDLVVELEA QLEPLAQESS LATDYVAQKR DFDQLDQTRL VLQIQDQKKA
     LKTGQETLAA KQAQIDRSKA ALADHHQALT ELKERQANLQ TQKDELQNQL LDLTKRHQEL
     VGQQALTQER QNHRQETIAN LTDRVKTVSD QRDGLTKQLA QCQATLKKEQ QALTAAKERV
     KQLAQQLAAL DTTAVSKEID HLQDDYIKAM QDLTSVHNQK AYLQKNQHRA DSESDRANEQ
     LQALKQELAT QTAKLQECQQ LVDQAQTALE TAKMRQTAAQ TNRQLRQQKA NQLNQQWLKA
     LEVSQRAKAR AKSLEEVAEN YAGFYQGTRA VLKARNQLNG IIGPVAELLQ VDSRYTKAVE
     AAIGSQQQNV VVETENAGKA AIQYLNQNRL GRSTFLPLTT IRAKSVDRQT QNLVSQLPGF
     LGVGSTLVTI AGDARMRILG DYLLGNVLFI DTLDHAVAIG KQLRQRYRMI TLDGDIISAT
     GAMTGGRSKR DSAGLLTQQQ ELSTLKTSIK QMDDQLTEKK RALDQLRQDD DQAALDRLNQ
     ALTTASTTYQ KRLNQSELIE QTINTLKRQI KAQTTQQALQ GDEEDFQQAL ADNERAEGEL
     NAQVAQMTAA MTAAKAQLTE NQTKSGSVSV ALQTEKETVA AKRVSVGQLQ RDVTEAQTQI
     QVADDQLSDF KNQLQDLTAT TTNTSASATS SKQQLAVLAD KQHEVESAIQ QNQAALADQA
     AKISELERTV QLATETYNIE QNEKQQAEFA QSRLTTKLDQ SLTTLSEQYH VSLELAVQQA
     VDLPLATIQQ RLKLLRRGLE DIGDVNVGSI ETYKQVKERY DFLTQQQADL NEAKQKLLTT
     MAEMDQEVIT RFEKAFNLVN AQFQKTFKQM FGGGRGRLEL TDPEHLLTSG IEIMAEPPGK
     RLQSMRLLSG GERALTAITL LFAIIQVQPV PYCVLDEAEA ALDPANTARF ASYLNRFQDD
     TQFIVITHRK ETMVQTDRLY GITMQESGIS KLVAVDLTKT AEIN
//
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