ID A0A1E8GKF1_9LACT Unreviewed; 1181 AA.
AC A0A1E8GKF1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=BG261_07175 {ECO:0000313|EMBL:OFI48667.1};
OS Floricoccus tropicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Floricoccus.
OX NCBI_TaxID=1859473 {ECO:0000313|EMBL:OFI48667.1, ECO:0000313|Proteomes:UP000178622};
RN [1] {ECO:0000313|Proteomes:UP000178622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF1 {ECO:0000313|Proteomes:UP000178622};
RA Chuah L.-O., Yap K.-P., Thong K.L., Liong M.T., Ahmad R., Rusul G.;
RT "Draft genome sequence of a novel species of the family Streptococcaceae
RT isolated from flowers.";
RL Submitted (SEP-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:OFI48667.1}.
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DR EMBL; MKIR01000024; OFI48667.1; -; Genomic_DNA.
DR RefSeq; WP_070793058.1; NZ_MKIR01000024.1.
DR AlphaFoldDB; A0A1E8GKF1; -.
DR STRING; 1859473.BG261_07175; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000178622; 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; 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; 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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000178622}.
FT DOMAIN 517..636
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 166..200
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 240..453
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 676..911
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 1181 AA; 133788 MW; F7A33C54CA147ABD CRC64;
MFLKKIEMIG FKSFADRTKI QFDQGITAIV GPNGSGKSNV TESLRWALGE QSAKSLRGAK
MPDIIFAGTQ NRKALNFAEV IVTFDNEDKY LNSEKEVSIT RRLYRNGDSE FLINGKKVRL
KDVHDLFTDT GLGRDSFSII SQGKIESIFN SKPEERRAIF EEAAGVLKYK GRKKETESKL
NSTQENIDRL DDILYELNTQ LAPLKAQRDT ALKYQGLEEE RVKLELSVVV AQIIKEKVSY
DEREESLEKI KKELSEIAEK QKKFELTNSS IKDKRQKLEF QKEELQTEVV SLTRLKSDYQ
GKIELFDSQK NASDKSKAEV EERLKTAEID KIDYQEKLKE VQISIEENEL QKSILEKELI
ALEIEQGKYS DSPEVIMEQL RTDYVDLVNK EAEITNQITR NKAEIDNILR TTREQNENSQ
QLEEKFAENQ RLLEQSKMEV EKSKLDVEGL LDEYKKIASA QSLAGQEFQK AQNAMFDQLD
ILKNQRAKLT SLENIQANHS NYYQGVKAVL QNADNIGGIV GPVADLISFD SQYATAMEIA
LGAGAQNVIV EDENSARKAI DYLKKSRQGR ATFLPLTSIR ERELSQNNIN KLQGMNGFID
VALNLVEFET RIFKALSSLL GTTAIVDTTE NASQIAKALN YSVRIVTLDG TLLMPGGSYS
GGAGKRNSTT FTVAEIDNLK KTLPQLEETL RTAELKVQEL QNKRDSLTTE LENIRQAGEM
ARLASQEKQI KLEQLQKEEE DFKIQLSFIS TSKDSLELES LTNKNKELEQ ELSGIAIKKV
KIDGDLSQIR ENQADLKLIQ DKLQNDIQET RLKLSEVSSE LRFSATELSR LERELEDTLA
EIKGLTLSLT EPSDLSLEER DNLSSKLVEV EERLESCNRK IIQIKFESED LQAQLDDLED
ANAENINLRQ IVGDKRTRLE MELEQSKNYL LSRQSLLTDN YHMSFEEAKD KSTDIEDLKQ
SEMKLRDLEK AIRSLGVVNL DAISQYEEVS TRYDFLNTQK EDLLQSKEML LTTISDMDEE
VKVRFKTTFE AIRESFKTTF TQMFGGGNAD LELTSDDLLE AGVEIAVQPP GKKLASLNLM
SGGEKALTAL ALLFAILRVR TVPFVVLDEV EAALDEANVK RFGDYMSRFD GASQFIVVTH
RKGTMAAADV MYGVTMQESG ISKIVSVKLK DIDEKILEEE K
//
