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Database: UniProt
Entry: Q87YY4_PSESM
LinkDB: Q87YY4_PSESM
Original site: Q87YY4_PSESM 
ID   Q87YY4_PSESM            Unreviewed;      1162 AA.
AC   Q87YY4;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   OrderedLocusNames=PSPTO_3658 {ECO:0000313|EMBL:AAO57127.1};
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO57127.1, ECO:0000313|Proteomes:UP000002515};
RN   [1] {ECO:0000313|EMBL:AAO57127.1, ECO:0000313|Proteomes:UP000002515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA   Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA   Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA   D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA   Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA   Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO57127.1; -; Genomic_DNA.
DR   RefSeq; NP_793432.1; NC_004578.1.
DR   RefSeq; WP_011104654.1; NC_004578.1.
DR   AlphaFoldDB; Q87YY4; -.
DR   STRING; 223283.PSPTO_3658; -.
DR   GeneID; 1185323; -.
DR   KEGG; pst:PSPTO_3658; -.
DR   PATRIC; fig|223283.9.peg.3748; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_6; -.
DR   OrthoDB; 9808768at2; -.
DR   PhylomeDB; Q87YY4; -.
DR   Proteomes; UP000002515; Chromosome.
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; 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|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:UP000002515}.
FT   DOMAIN          520..615
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          170..238
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          300..334
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          363..432
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          456..500
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          656..907
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   1162 AA;  131541 MW;  00E19FF4C292DBC6 CRC64;
     MRLKCIKLAG FKSFVDPTTV NFPSNMAAVV GPNGCGKSNI IDAVRWVMGE SSAKNLRGES
     MTDVIFNGST SRKPVSQASI ELVFDNSDGT LVGEYAAYAE ISIRRKVTRD SQNSYYLNGT
     KCRRRDITDI FLGTGLGPRS YSIIEQGMIS KLIEAKPEDL RNFIEEAAGI SKYKERRRET
     ENRIRRTHEN LARLTDLREE LERQLERLHR QAQAAEKYQE YKAEERQLKA QLSALRWQAL
     NEQVGQREAV IGNQEVGFEA LVADQRSADA SIERLRDGHH DLSERFNLVQ GRFYSVGGDI
     ARVEQSIQHG QQRLRQLQDD LREAERARLE TESHLGHDST LLATLGEELE MLEPEQEMTS
     AAAEESAIAL EDAESAMQGW QEQWDVFNQQ SAEPQRQAQV QQSRIQQLEQ SIERLAERQR
     RLAEERQLLT ADPEDAAILE LSEDLATRDM TLEELHMGEE QTVERLEQLR EALQNASHAQ
     QQAQGELQRL NGRLASLEAL QQAALDPDTG TAEWLRDQQL AERPRLAEGL SVEAGWELAV
     ETVLGADLQA VLVDDFDGLD LASFQQGDLR LLSASADTVR VPGSLLEKVE STVDLSAWLG
     QVMPVENLDE ALARRTQLSA GQSLISRDGY WVGRHFLRVR RASEAQSGVL ARGQELQRLG
     LERDEREATL ASLEEQLLSL REQQSQQEDA REQLRRRVQD ETRQQSELKA QLSAARVKVE
     QLTLRRTRLD EELAELGEQR SVEHEHLGES RLQLQDALDS MALDTEQREV LQAQRDALRE
     RLDRIRQDAR QHKDHSHQLA VRLGSIKAQY DSTRQALERL RMQSERLTEK REQLSLNLEE
     GEAPLEELRL KLEELLERRM VVDDEMRIAK NALEDADREL REAEKRRTQA EQQSQLLRGQ
     LEQQRLEWQA LSVRRTALQD QLHEDGYDLH GVLATLTSEA SEQAAEQQLE SIAGRIQRLG
     AINLAAIDEY QQQSGRKRYL DAQDADLVEA LDTLENVIRK IDKETRNRFK DTFDQINSGI
     QALFPKVFGG GSAYLELTGE DLLDTGVTIM ARPPGKKNST IHLLSGGEKA LTALALVFAI
     FKLNPAPFCM LDEVDAPLDD ANVGRYARLV KEMSQTVQFI YITHNKIAME MADQLMGVTM
     HEPGCSRLVA VDVEQAMALV DA
//
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