ID A0A1G1PYY7_9BACT Unreviewed; 1134 AA.
AC A0A1G1PYY7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=A2243_05740 {ECO:0000313|EMBL:OGX46834.1};
OS Omnitrophica WOR_2 bacterium RIFOXYA2_FULL_38_17.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801873 {ECO:0000313|EMBL:OGX46834.1, ECO:0000313|Proteomes:UP000179162};
RN [1] {ECO:0000313|EMBL:OGX46834.1, ECO:0000313|Proteomes:UP000179162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGX46834.1}.
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DR EMBL; MHHG01000073; OGX46834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1PYY7; -.
DR Proteomes; UP000179162; Unassembled WGS sequence.
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; 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; IPR011890; SMC_prok.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_01894}.
FT DOMAIN 2..1113
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 167..272
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 311..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 711..829
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 885..949
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 1134 AA; 130509 MW; 11BF3BEC2B037AFA CRC64;
MYLKRLEIFG FKSFADKTVL NFEPGITAVV GPNGCGKSNV FDSIRWVLGE QSAKELRGSA
MGDVIFNGTE KKASLGFAEV SLTFSNESKM LPIDYDEVTI TRRLFRSGES EYLLNKTPVR
LKDIQELLMG TGIGAEAYSL LPQGKVDMVV SAKPEERRMI LDEASGITKY KAKKKEALNR
LKDTENNLLR VNDITIEVKR QIASIERQAK KASKYKEKFE FLKKQETKYS RCQIKELEDE
KSSMDVHVKE VTEKINSLNQ ELEEASEHLT NEINYLGEVE HKINELNSQG IKLDGQIDLD
NRQVGFNQER IENLMQNDRK LKEQKGQLIE KCKIQQEKIE ELEQALITLE EAKIHNERSL
KEKRDVLAIL ERLVKEAKDK IKGNEENILS LSAKQANTRN DLTDVMKEMQ GYLARKRRLE
LETEKVLIEK QQVNERLDEV NGQINSLDLE INEFKQIKDS RGEKLRSYEA EFEQLKSTIE
DLEKKTLFLK SQKEFIEKLH AQYQDMPDPV VEGRYYASAA PMDHHTGIIG KVKEVNALAD
DQLQQLKQRF NQSVGNGLEQ SLQLYEIVCE TKFVELDPQQ ISLKINEINL QISEYVARRD
FVSGQIVEHR ELFKEVIYKI QDKEKKHSIL ESQRNDILAE EQKLQGEMEL VCSEIEEVKE
FMAETKKNEE RISYELETIT QDIEWCQNDI HDKREAIASK SKEKENVIVS IAQLETEIAA
DSDKLTSYKK NQSMFSETLD GWLEDINKID NEAIGQEDKK SLYEREIEGL ERRIEEVRSE
RESFKNVLND YIVQKEDIAQ RINSSRANMN ALELEIDDIK QKVHEKQLKE QEISFSIRAI
KDRMSQTYKI DLDAPERDMN TSFSEKDATQ CPLIQLEAEI FGKVLEVKEL KAEKAFEEVE
EQAEQIDMNE LALEIEKLRK QCDSFGSVNL VAIEEYEQLK ERFEFLTKQQ SDLFEAKSQL
MSTINKINRS TRQMFMETFT KVSEQFRIYF RMLFGGGEAQ LVLLEPDNVL ESGIEIIARP
PGKKLQSISL LSGGEKTLTA IALIFGVFKV NPSPFCVLDE IDAALDESNV GRFGFLLKDF
AKIAQFIVIT HNKKTIANAN IMYGITMPET GCSRVVSVKF SSEEKQEEVL TAGV
//