ID A0A261G0Z6_9BIFI Unreviewed; 1232 AA.
AC A0A261G0Z6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=BAQU_1830 {ECO:0000313|EMBL:OZG65090.1};
OS Bifidobacterium aquikefiri.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1653207 {ECO:0000313|EMBL:OZG65090.1, ECO:0000313|Proteomes:UP000216451};
RN [1] {ECO:0000313|EMBL:OZG65090.1, ECO:0000313|Proteomes:UP000216451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28769 {ECO:0000313|EMBL:OZG65090.1,
RC ECO:0000313|Proteomes:UP000216451};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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. {ECO:0000256|HAMAP-
CC 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:OZG65090.1}.
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DR EMBL; MWXA01000009; OZG65090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261G0Z6; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000216451; 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 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:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000216451}.
FT DOMAIN 507..636
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 955..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 319..484
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 680..839
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 868..902
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1018..1066
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 968..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1232 AA; 136372 MW; FEFEA84A8176E912 CRC64;
MYLKDLSLRG FKSFASATTL RFEPGITAVV GPNGSGKSNI VDALAWVMGE QGAKTLRGTS
MEDVIFAGTS SRPPLGRAQV SLTIDNTDHA LDIEYSEVTI TRTIFRNGGS EYSINGTSCR
LLDIQELLSD TGLGSQMHVI IGQGRLDSIL RADPAGHRAF IEEAAGILKH RKRKERALRK
LANTETNLSR LDDLLSEIHR QLGPLGRQAR ISRRADGIQI ALRDAQSRLL AEDAVTLSSR
RDTVRAELTK ARGALVAQQR ELVTIKSQIE QIESLSSTTS PEMRELNDGF NELTRIQERL
RSLQSLAHER SESALGRIQQ AVGDDSQMLR NRAEELEQQG KAQQRLIDDA RLKFDRTTEE
RAGFEKHLAS VRQTLNELRQ STQQRERQLS KLREMIAREQ SALQLSQSRA KDFEGQIGNL
RQQLGDLETR HTEMRAQSEH MDAQDLDDQL AKAQKSYEAE GLKLNEANER QRKINGRIIS
LQAKADALND TLESRNASGA LEKDDAIDVM GKLADFIHVK TGWEEPVAHA LDVFANAVVV
PDAEQIDRAL QHVRDNNLGK AVLISPSSGT AINESLGDFD TANPHQSGFS SLAQYISVRE
SSGVDHQMAV SILQSVRMLL SDVAAVDSLE QARSAIHDGW QQAVTADGDV VNAVGASGGS
SLSQSDLALV SRRDAALKQV KEMDATLDEL TTSVKHLSEE HSAARSILES LRNKRTEVQL
RLKQMRDSLN DLQRRITQFG HQIHDAETKS SQAHDDAHNH AVKLDDLQEA LNEAERSSDG
QASFDELGQR EKSLEASLAK TREQEVTAKI AWNEAVSKAE SLTRQSQMLR DNAKSADERR
IRIQRKNAVL QAQYDNSLAV ARATQQVINL VEAAVSSAQE KRDALQSAAS EHDAQLKDLR
ALRDGKEPQV GALQQQEHAL DIERERLATQ FGQLTQKVSD ELGLNLTELI DGFGPDKQIP
VLDETGKPKL LDGSDEESRD DQPRESEDRS VKDGQISGAD PQHAASPDER IMTIPYSREE
QQSRLEKAQR DLARLGKVNP LAAEEYESLE SRNAFLNKQR NDVTQSRDDL MSLVKNLDAT
MMDVFRTAFE DTAQAFTKVF STLFPGGTGR LRLEDPDDLL HTGVIVEASP AGKRVKQLSL
LSGGERSLTA LALLFAIFTA RPSPFYVMDE VEAALDDVNL TRLLNALQDL RSHAQLIVIT
HQQRTMSIAD ALYGITMRDD GVTAVISQKM SH
//
