ID A0A0M4LVN4_9SPHN Unreviewed; 1140 AA.
AC A0A0M4LVN4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=AMC99_01630 {ECO:0000313|EMBL:ALE16921.1};
OS Altererythrobacter epoxidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=361183 {ECO:0000313|EMBL:ALE16921.1, ECO:0000313|Proteomes:UP000057938};
RN [1] {ECO:0000313|EMBL:ALE16921.1, ECO:0000313|Proteomes:UP000057938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7731 {ECO:0000313|EMBL:ALE16921.1,
RC ECO:0000313|Proteomes:UP000057938};
RA Li Z., Cheng H., Huo Y., Xu X.;
RT "Complete genome sequence of a benzo[a]pyrene-degrading bacterium
RT Altererythrobacter epoxidivorans CGMCC 1.7731T.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01894}.
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DR EMBL; CP012669; ALE16921.1; -; Genomic_DNA.
DR RefSeq; WP_061925139.1; NZ_CP012669.1.
DR AlphaFoldDB; A0A0M4LVN4; -.
DR STRING; 361183.AMC99_01630; -.
DR KEGG; aep:AMC99_01630; -.
DR PATRIC; fig|361183.4.peg.1602; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000057938; Chromosome.
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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000057938}.
FT DOMAIN 3..1124
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 456..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..335
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 1140 AA; 123514 MW; 9EBFC9DAD21A1272 CRC64;
MEISRLKLSG FKSFVEPAEL RIEPGLTGVV GPNGCGKSNL LEAIRWVMGE NSPKSMRSGG
MEDVIFAGTE SRPARDFAEV VLQASDSEGE ELEVTRRIER GAGSAYRVNG RDVRAKDVAL
TFADAATGAH SPALVSQGKI AQVIAAKPTE RRQMLEEAAG IAGLHVRKKD AESKLKSTEK
NLERLEDLMA GLDAQMSSLR RQAKQAERYK KLSDEIKVAE ARLLYARWRD AAAAADEARK
AAKTADEKVA QAKVASDEAQ KAQAAAAAAI AEAREELADR RDDASAHGHR MAALSSQLEA
AEQRLADLDR QKIRLEEDRG NADRLTRDAA EALARLERDL VASVKALEAD EARRPALLAK
SEDTERASRT AELALAKATA DHAGVEAEWR VAEAEITQAE NRLARLRSDS ERHERTRAEL
GASGDPEIAV SEAQAAAKQA AGKLVQLRAR LEQAQSRKSD LQERRDQAST ALSSAKAELA
GIEREYNALA RDRDARERQA EQRKGLPTAL DKLGVEPGYE RAIAAVLGRD AKSPLGKPAQ
DTDGRFWTGT DAPKAVADSV LDHVTQCPQE LKARLALVHV ADSDDGRDLG PGEWLVTLAG
HLRRWDGFIA RGEGAAEAAR LEAANRLAEL EGQLPSLRTA IEKAETEEQE ARDALSALGA
DLVAQERGIA AAIEDERHAL RALDQAEAAR ERLAARLAEL ADAEKDLAEQ LAQAEKELKS
AQDKRAALPP PDAGRAQLEA AQAKHEAAKS AVQSAAAELA AHDQGLAVAR ERTAAQRSEK
SNWEQRSGEA AARMADTANR LEEIEQERAV VAAKPEGLIK EIEQGDVMRA KLGEELAAAE
RIVAERQETL NQADRNFAET NEALATARES RAGLAARAEN EEARRGEMAR ISGERFQCPP
PMLAERFDFE PGQIGKAGAE AEEMDRLTAS RERIGPVNLV AADELARIEE EHGASASEQA
ELVEAVNRLR GSIGNLNREG RERLRAAFDE VNGHFQRLFV RLFQGGSAHL ALIDSDDPLE
AGLEIFAQPP GKKLQSLTLL SGGEQALTAT ALIFALFLTN PAPICVLDEV DAPLDDANVE
RFCDLLDSMV RETRTRYLIV THNAVTMSRM HRLFGVTMAE KGVSRLVSVD LGEAELMAAE
//
