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Database: UniProt
Entry: M7MXW7_9BACT
LinkDB: M7MXW7_9BACT
Original site: M7MXW7_9BACT 
ID   M7MXW7_9BACT            Unreviewed;      1178 AA.
AC   M7MXW7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN   ECO:0000313|EMBL:EMR01268.1};
GN   ORFNames=ADICEAN_03617 {ECO:0000313|EMBL:EMR01268.1};
OS   Cesiribacter andamanensis AMV16.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC   Cesiribacter.
OX   NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR01268.1, ECO:0000313|Proteomes:UP000011910};
RN   [1] {ECO:0000313|EMBL:EMR01268.1, ECO:0000313|Proteomes:UP000011910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMV16 {ECO:0000313|EMBL:EMR01268.1,
RC   ECO:0000313|Proteomes:UP000011910};
RX   PubMed=23682146;
RA   Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT   from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL   Genome Announc. 1:E00240-13(2013).
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:EMR01268.1}.
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DR   EMBL; AODQ01000130; EMR01268.1; -; Genomic_DNA.
DR   RefSeq; WP_009196997.1; NZ_AODQ01000130.1.
DR   AlphaFoldDB; M7MXW7; -.
DR   STRING; 1279009.ADICEAN_03617; -.
DR   PATRIC; fig|1279009.4.peg.3660; -.
DR   eggNOG; COG1196; Bacteria.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000011910; 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; 2.
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|HAMAP-Rule:MF_01894};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011910}.
FT   DOMAIN          520..632
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          167..215
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          297..485
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          671..787
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          879..934
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   1178 AA;  134324 MW;  0CB62065619253ED CRC64;
     MRLTRLEIKG FKSFGDKVVI NFDEGITGIV GPNGCGKSNV VDAIRWVLGE QKTKALRSDK
     MENVIFNGTK HRKPSQLAEV SLTFDNTKNL LPTEYSRVTI TRRYYRSGES EYELNGVACR
     LKDISNLFLD TGIASNSYAI IELKMVDELL NDKEGSRRAL FEEAAGISKF KKRKKETLRK
     LEETNADLER VKDLLFEIEK NLKSLERQAK QAERYFALKE DYKKLSLRLG RLAISQSTER
     FLGLHKQLEA EQDRKGALDA QLAEREALAE ESKAQLLGRE KLLSSRQKTL NEHVSKIRQV
     ESDKKIKNER LRFLNDKRDS LLEQLQSDKQ SYERAAFSLN GLAQERSEAE ALATEAKALL
     DELREAHDEQ KSITTALREE AATATNQQRQ LQEQAFKLSK SLEIKQMQLS SLRQELEKTA
     QEGSQHSNSL SQFEDKLADV QEAVAEKEQE LQQLQADEGQ MQQQLAELEQ GLNQNREALA
     ADRRQLDARQ NEYNLTKSLV DNLEGFPEAI RYLKKKTDWG RNVPLLSDII TCSEAYRVAI
     ETYLEPWMNH YVVDSWQQAQ EAIALLSEAA RGRAQFFVLE ALPPASPSPT TPPAGCTPAL
     SVVEADPKYA PLTAHLFADT YLCEDAEMET IGSSAYSLIS RSGRIIKRRY SLLGGSVGMF
     EGKRIGRAKN LEKLQKDIQQ LLSEVSRLEK LQQEQHTELG RLKSSTRRPQ IEAVSRELSL
     LQQELVQVRT RHEQLLQLLS NQATRQDDMR QQMEVLQDEI ADIDPEAAAV AERLQALEAR
     SIQLQDDLAY QNEALSVKSA RFNEQNLLYH QKENKLNSLV QEMGFKQQSL QSSEERISRN
     KSSLADTEAE IEGLMQRGEL GDEELMAMYS EKESIEAGVN EAERDYYEMR GQIDALEKEA
     RELQRRRESS QALMMELQNR QNEYKLQLTS VKERLAVEFN VDAEELMEAP AVDELLSEAE
     LQQEVRQVRE KIDKIGPINP MAMEAYQEIQ ERYQFITAQR DDLVKAQESL LETMAQLDSA
     AQEAFLSAFE QIKENFVKVF RSLFTEEDDC DLRLTDPSNP LETTIDIIAK PKGKRPLTIN
     QLSGGEKTLT ATSLLFSIYL LKPAPFCIFD EVDAPLDDAN IDKFNNIIRK FSQDSQFIIV
     THNKRTMAST DIMYGVTMLE MGVSRVVPVD LRELEVEF
//
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