ID A0A087A9H7_9BIFI Unreviewed; 1220 AA.
AC A0A087A9H7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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=BCAL_0683 {ECO:0000313|EMBL:KFI55427.1};
OS Bifidobacterium callitrichos DSM 23973.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437609 {ECO:0000313|EMBL:KFI55427.1, ECO:0000313|Proteomes:UP000029072};
RN [1] {ECO:0000313|EMBL:KFI55427.1, ECO:0000313|Proteomes:UP000029072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23973 {ECO:0000313|EMBL:KFI55427.1,
RC ECO:0000313|Proteomes:UP000029072};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-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:KFI55427.1}.
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DR EMBL; JGYS01000005; KFI55427.1; -; Genomic_DNA.
DR RefSeq; WP_043167006.1; NZ_JGYS01000005.1.
DR AlphaFoldDB; A0A087A9H7; -.
DR STRING; 1437609.BCAL_0683; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000029072; 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; 1.20.5.340; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 6.10.140.1720; -; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW 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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01894}.
FT DOMAIN 506..636
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 679..769
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 888..950
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 1220 AA; 133017 MW; 9E4A0F4388B69AC6 CRC64;
MYLKELTLKG FKSFASATTL RFEPGITAVV GPNGSGKSNI VDALTWVMGE QGAKNLRGAS
MEDVIFAGTS SRPALGRAQV SLTIDNTDHT LDIDYDEVTI SRTIFRNGGS EYAINGSPCR
LLDIQELLSD TGLGQQMHVI VGQGRLDSIL KADPAGHRAF IEEAAGILKH RKRKERALRK
LANTETNLSR LDDLLGEIRR QMGPLGRQAR VSRRADAIQI TLRDAKSRLY ADDAVTSTAK
RDDVRAELTR VRGELTASRR SLARIKVSIE QAEASISSSS PALDRLNRTW RSLMQIQERL
RSLSALADER GDSLLRQVID NPGEDPTILE HRAVELDEQA AAQSAVADNA RIALDKATEG
RAADEQRLAA VRQTLIELRR TQQERGERIA GLREMIAREE GAVQLGAGRV RDLETQLAAL
VEEHGEAVGL RARLKGESDP DGDDGSEALD AAHTRLADSR DALGELLDRR RELGARVISL
EAKADALKDT LENRNAAGAL ESDVQAGVLG RLTDFIHVAD GWEEAVAHAL GRYASALVVP
DGTHMLHALE RARVDRLGRA VVVNASGEAA SASSAPASSV PASASDKTAA TSLASLIEAD
PDASDPALAA RVVDAVRALI GDYVIAEDAE TAQRMVSDTA SSRPGMHAVT REGEVFADGV
AASGGSSLSQ SDLTLNAKRN RALKQVRELN VELAKLDAEV KSAQAVRDEA ARMVDQAVQR
RTERRLRARQ AEASLKEAND RVAALERRIA DLKDRIERID VECASHRERL DDLNGMLEAA
GHADDGDADV DGLTERERAL ESALSLARDQ ETAARIAWTE SSRKAESLAR QAGLLHANAK
EAAERRARVE TVNAARRQQA EQARNVARDA RGAETLVAEA IADVVDRRDR LQAAASGRNE
ELRALREQRN AIEPTVGELA AREHELDVVR ERLASEHDQL EARIRDELAM GVEDLIAEYG
PDRPVPVLDE TGAPIPLETP DDDAYDTDAD DAADIRYRTT PYVRAEQERR LEKAKRDLTA
LGKVNPLAVE EYAALEERNR YLNEQRDDVA RSRDDLMGLI DELDRTMVGV FRTAFDDTAK
AFESMFATLF PGGTGRLRLE NPDDMLTTGV IVEASPAGKR VKRLSLLSGG ERSLTALALL
FAIFTARPSP FYVMDEVEAA LDDVNLTRLL NALNRLREHA QLIVITHQQR TMSIADALYG
VTMRSDGVTA VISQRITNPA
//
