ID A0A0F7KP39_9SPHN Unreviewed; 1141 AA.
AC A0A0F7KP39;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc_2 {ECO:0000313|EMBL:AKH42288.1};
GN Synonyms=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=FHS61_000058 {ECO:0000313|EMBL:MBB5731065.1}, WYH_01243
GN {ECO:0000313|EMBL:AKH42288.1};
OS Croceibacterium atlanticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH42288.1, ECO:0000313|Proteomes:UP000034392};
RN [1] {ECO:0000313|EMBL:AKH42288.1, ECO:0000313|Proteomes:UP000034392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26DY36 {ECO:0000313|EMBL:AKH42288.1,
RC ECO:0000313|Proteomes:UP000034392};
RA Wu Y.-H., Cheng H., Wu X.-W.;
RT "The complete genome of Altererythrobacter atlanticus strain 26DY36.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5731065.1, ECO:0000313|Proteomes:UP000556014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100738 {ECO:0000313|EMBL:MBB5731065.1,
RC ECO:0000313|Proteomes:UP000556014};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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}.
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DR EMBL; CP011452; AKH42288.1; -; Genomic_DNA.
DR EMBL; JACIJL010000001; MBB5731065.1; -; Genomic_DNA.
DR RefSeq; WP_046903138.1; NZ_JACIJL010000001.1.
DR AlphaFoldDB; A0A0F7KP39; -.
DR STRING; 1267766.WYH_01243; -.
DR KEGG; aay:WYH_01243; -.
DR PATRIC; fig|1267766.3.peg.1253; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000034392; Chromosome.
DR Proteomes; UP000556014; 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 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:UP000034392}.
FT DOMAIN 3..1124
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 275..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 613..758
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 822..884
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 407..425
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 1141 AA; 124082 MW; 8753E1C93975FEBA CRC64;
MLIRKLKLSG FKSFVEPAEL RIDPGLTGVV GPNGCGKSNL LEAIRWVMGE NSPKSLRSGG
MEDVIFAGTA RRPQRDFAEV VLHATDGEGE ELEVTRRIER GAGSAYRVNG RDVRAKDVTL
VFADAATGAH SPALVSQGKI AQVIAAKPAE RRMMLEEAAG IAGLHVRRRD AENKLRQTEA
NLARLEDLMA GLDSQMNSLR RQARQAERYK ALSEKILLAE ARLLYARWRD AAAAAEAARA
QAKQAEAHVA AMQAATTQAQ KTQAELAQNL ARARDELADR RDDSSAHGHR MAALSSQLEA
AEQRLADLDR QKARLEEDRG EADRMTRDAA EALSRLEQEL NAGRKALETD EARRPEIAAR
TEDAERAART AELALARATA DHAGVEAEWR VAEAEVAQAR SRIERLDQEA RRQDDLRRSL
GEQGDPDEAV AEAQSAVEEA SRKLAELREA IEAKRARKDE LGAERDEASS ALSSAKAELA
GIEREWQALK RDREARARQA SGKHGLPPAI DRLSAAPGYE RALAAVLGRD AKAPLGLPDA
EAEGRFWTGS AVPARVADSL ADHVTACPPQ LAARLALVHV VPADDGRELK PGEWLVTTGG
HLRRWDGFIA RGEGAAEAAR LEAENRFKEL EKQLPPLREA AERAEKRQQE LQEMLAALQR
DLISGDREIA QASDAERGAL RALDQAEAAR ERLAARLAEL DESAADLAEQ RAAAQKDLEA
AEARRAVLPD PETGRATLAA AQARNEAART AMQAAAAALA SHDQALAVAR ERVGTQQADI
KGWQARAGDA ARRLSGMEQR FEEIAEERVV IAAKPEGLMR EIEGGEAVRE RLAAELAKAE
ADVARIAEEA RQADAALAQA NEKLATAREE RAGAAARAEN EESRREEMAR ISGERFQCPP
PILASRFDFE PQDIAAHAEE SAILDKLSSD RERIGPVNLV AAEELAKIEE EHGSSAAEQA
ELAEAVNRLR GSIGSLNREG RERLRAAFNE VNEHFQRLFT RLFEGGQAHL ALIDSDDPLE
AGLEIFAQPP GKKLQSLTLL SGGEQALTAV ALIFALFLTN PAPICVLDEV DAPLDDANID
RFCDLLDQMV NETQTRYLIV THNAVTMSRM HRLFGVTMVE RGVSRLVSVD LGGAEELLAA
E
//
