ID Q9I3I6_PSEAE Unreviewed; 1162 AA.
AC Q9I3I6;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=PA1527 {ECO:0000313|EMBL:AAG04916.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG04916.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG04916.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG04916.1; -; Genomic_DNA.
DR PIR; D83454; D83454.
DR RefSeq; NP_250218.1; NC_002516.2.
DR RefSeq; WP_003114676.1; NZ_QZGE01000032.1.
DR AlphaFoldDB; Q9I3I6; -.
DR SMR; Q9I3I6; -.
DR STRING; 208964.PA1527; -.
DR PaxDb; 208964-PA1527; -.
DR GeneID; 879466; -.
DR KEGG; pae:PA1527; -.
DR PATRIC; fig|208964.12.peg.1580; -.
DR PseudoCAP; PA1527; -.
DR HOGENOM; CLU_001042_2_2_6; -.
DR InParanoid; Q9I3I6; -.
DR OrthoDB; 9808768at2; -.
DR PhylomeDB; Q9I3I6; -.
DR BioCyc; PAER208964:G1FZ6-1554-MONOMER; -.
DR PHI-base; PHI:7016; -.
DR Proteomes; UP000002438; 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:UP000002438}.
FT DOMAIN 520..615
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 306..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 363..500
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 649..907
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 980..1007
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 315..337
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 1162 AA; 131581 MW; A62DCDC73D15ACB5 CRC64;
MRLKSIKLAG FKSFVDPTTV NFPSNMAAVV GPNGCGKSNI IDAVRWVMGE SSAKNLRGES
MTDVIFNGSN TRKPVSQASI ELIFDNAETT LVGEYAQYAE ISIRRRVSRD GQNTYFLNGT
KCRRRDITDI FLGTGLGPRS YSIIEQGMIS KLIEARPEDL RNFIEEAAGI SKYKERRRET
ESRIRRTQEN LARLTDLREE LGRQLERLHR QAQSAEKYQE HKAEERQLKA QLGAVRWRDL
NEQVGQRERV IGDQEIAFEA LVAEQRGADA GIERLRDGHH ELSERFNQVQ ARFYSVGGDI
ARVEQSIQHG QQRQRQLQDD LREAERTRQE TESHLGHDRT LLATLAEEMA MLAPEQELSA
AAAEEAGIAL EQAEQGMQAW QQQWDAFNQQ SAEPRRQAEV QQSRIQHLEQ SLERLQDRER
RLQEERGQLA ADPEDAAILE LNEQVAIAEL ALEELQLQEQ GQAERLEQLR QELQQLAAEQ
HQAQGELQRL NGRIASLEAL QQAALDPGQG ALEWLREQGL EQRPRLAEGL RVEPGWELAV
ETVLGADLQA VLLDGFDGLA LAGFGKGELR LLSPARGAAT AAGSLLDKVR ADADLSPWLA
RVKPVETLEQ ALAQRGALDD GESLISRDGY WVGRHFLRVR RSDEAQGGML ARAQELEALQ
ERREALETRV AEGEERLAAA RDEQRELEGA REQVRRQVQE EGRRHGELKA QLSAQQAKVE
QLVLRRRRLD EEVAELAEQR ALEQEQLSEA RLTLQEALDS MALDTERRES LLAERDALRE
RLDRIRQDAR THKDHAHQLA VRVGSLKAQH NSTQQALERL DQQSARLNER CEQLNLNLEE
GAAPLEELRM KLEELLERRM AVEDELKQAR LALEDADREL REVEKRRGQA EQQSQLLRGQ
LEQQRLEWQG LVVRRKALQE QLAEDGYDLH TVLANLPLDA SERDWEERLE SLAARIQRLG
PINLAAIEEY QQQSERKRYL DSQNDDLAEA LETLENVIRK IDRETRNRFK ETFDQINAGL
QALFPKVFGG GTAYLELTGE DLLDTGVAIM ARPPGKKNST IHLLSGGEKA LTALALVFAI
FQLNPAPFCM LDEVDAPLDD ANVGRYARLV KEMSEKVQFI YITHNKIAME MADQLMGVTM
HEPGCSRLVA VDVEEAVALA EA
//
