ID A0A1E8YBX0_9LACT Unreviewed; 1185 AA.
AC A0A1E8YBX0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-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=HMPREF2811_08240 {ECO:0000313|EMBL:OFK53614.1};
OS Globicatella sp. HMSC072A10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Globicatella.
OX NCBI_TaxID=1739315 {ECO:0000313|EMBL:OFK53614.1, ECO:0000313|Proteomes:UP000176615};
RN [1] {ECO:0000313|EMBL:OFK53614.1, ECO:0000313|Proteomes:UP000176615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC072A10 {ECO:0000313|EMBL:OFK53614.1,
RC ECO:0000313|Proteomes:UP000176615};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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}.
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DR EMBL; KV805779; OFK53614.1; -; Genomic_DNA.
DR RefSeq; WP_071408911.1; NZ_KV805779.1.
DR AlphaFoldDB; A0A1E8YBX0; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000176615; 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; 1.10.287.1490; -; 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; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000176615}.
FT DOMAIN 518..637
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 283..475
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 721..916
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 1185 AA; 135657 MW; 6F1441641D2D3EDF CRC64;
MYLARVEMTG FKSFADKTVI EFDKGLTAVV GPNGSGKSNL SEAIRWVLGE QSAKSLRGSK
MEDVIFNGTQ DRKAVNLAKV TLVLNNEDRY LDYDFSEISI TRSYNRNGES NYYINNESVR
LKDIVDLLLD SGLGKNSFAM ISQGKVESIF LNKPEERRAI FEEAAGVQKY QFRKAEAERK
LIKSEDHLSR VKDIIHELEG QIKPLKKQRE TALKYQTYQE ELSSLEISLY THQIEQNRIK
WDEAQEKLSN VDQAIQLDEE ELTNLSETII EQQQMLDDLL ISIDRENETH QELVRKVEQA
KAKYQMLQQE LQFNQANTDE KTLQFENQLV QKERIQEDLA KQSTSKVTLE TEIEQLTDKI
SQLESDRKMA AGLSDDQVET LRGEMIQFYQ SEASAKNEVN LLEQQIEQQT MRLKRAKNKH
QMLKETLASS ETELKELETS LELKEATQKT QNEHHQSLQQ EWQALQQKRN QIQKELFAIE
RQVNTLNVRV NSLKQMQEQY DGYYGGVKFV MQHANDIGGI DGTVAELIHV KPEYQLAIDT
ALGGSLQHIV VEDDQSARKA IAYLKEHRAG RATFLPRPNI KGRSVQNYHL QPAQNHAGYI
GIGHQLVAFD EINQAIIENL LGNTIVMDTI VNAQSLSKQL RHQVKIVTLE GDILMPGGSI
TGGRQRNQQT SMLSRQTDLE KALIELEAAT NSQKSMITKI DQIEELEQSV RENGEASLNQ
VNQINHEVNQ QKQALQQFVQ QVKINQNELK VAQMDIDEAE QFINQSQAKL TEAQETIRLM
TQKIAEGTQQ LEQMNVSQAD RQKKIEQLNH ELSQLNTEKA VKQSELRQIK TQVEQLTAQL
VQLNEFIENY QNNQLSSEQD LNQLKETIME VESQIETLNN ELVEHTTKLD QSKQNRSEWN
QNLRDLENKK VKIQQQQQAQ FKLQAKLQAQ IEKFKELIDN HLNYLNEKYQ LSYEAASQQV
QTELAISEVS SRVKELRKAI DNLGPINLAA IEDFENLNER YTYLLEQQED LLTAMGQLQD
TMDAMDAEVI KRFSESFHQI NQQFKRTFKS LFGGGEASLE LTDPDNLLST GVDIIAQPPG
KRKQNLALLS GGERAFTAIA LLFAILETKP VPFCVLDEVE AALDDANVYR YGEYLQQFTE
NTQFIVITHR KGTMEHADVL YGVTMERSGI SKLASVRLSE ANNEK
//
