ID A0A0G3XKP1_9SPHN Unreviewed; 1141 AA.
AC A0A0G3XKP1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-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=AB433_12055 {ECO:0000313|EMBL:AKM11797.1};
OS Croceicoccus naphthovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM11797.1, ECO:0000313|Proteomes:UP000035287};
RN [1] {ECO:0000313|EMBL:AKM11797.1, ECO:0000313|Proteomes:UP000035287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PQ-2 {ECO:0000313|EMBL:AKM11797.1,
RC ECO:0000313|Proteomes:UP000035287};
RA Zeng Y., Huang Y.;
RL Submitted (JUN-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}.
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DR EMBL; CP011770; AKM11797.1; -; Genomic_DNA.
DR RefSeq; WP_047823989.1; NZ_JACIEL010000001.1.
DR AlphaFoldDB; A0A0G3XKP1; -.
DR STRING; 1348774.AB433_12055; -.
DR KEGG; cna:AB433_12055; -.
DR PATRIC; fig|1348774.3.peg.2537; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000035287; 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:UP000035287}.
FT DOMAIN 4..1124
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 344..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..262
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 627..758
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 479..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..892
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; 123133 MW; E0B95095C5F8BE74 CRC64;
MRFRRLRLSG FKSFVEPADL LIEPGLTGVV GPNGCGKSNL LEAIRWVMGE SSPKSMRGAG
MEDVIFAGAA SRPARSFAEV VLSTETDAGQ EMEVTRRIER GAGSAYRLNG RDVRAKDISL
MFADAATGAH SPALVSQGRI AAVIAAKPVE RRAMLEDAAG ISGLHVRRKD AEQKLRATEA
NLARLDDILS QLDSRIGSLR RQAKAAEKYK DLSAQIRTAE SRVLYARWRE AAAAADAARA
EAKRAEAAVA DAQSRTNAAQ GQQRVSAETL AKAREEMADR RDDLHAQANM LAVLTGKLEA
AEEKLADLDR QRARLDSDEG DANRTTRDAA EALSRLEREV KEAEKRLAAE EASRPERVAR
QERAEQEQRK GELALAQATA ELARVEADWR VADAAVTQAR GTLARLEQEM SQREAQGAAL
GDARELDLAL TNAQARCGKA EAAVGSAREA LDAARAERET MSLRRDEASS ALSAAKAELA
GVEREHDALE RDRRAREKAD KGNKGRTRAI DAVKAEPGYE RALAAVLGRD AAAPLGPPET
GQDGRYWTGA EAPKAVADSI AAHVRDAPAE LTARLAMVRI AESDDGQALT PGEWLVTRGG
ALRRWDGFVA RGEGAAEAAR LEAANRLEAL AEQLPALRAA VEDAESAVAD ANAALSDATD
ARIAAERAVN TASEEERAAL RARDQAENAV ERHSRAREEL AERLEEIHER LAAAQQEAMM
AEERRRGLPD PSAQQAALDT ARARNDAAKT ALQSAMAELA ALDQGLAVGR ERTKSLQSDM
KGWQARAGDA AKRLADMTRR REEIEEERAI TAARPEALLR EIEMAEKARD RLSEELGEAE
KVFTSAEAAG READALFAAA NEALANAREA RAGSTARAEN EEARRSEFAR TSGERFHCPP
PILPERLDFA SDSVAHADAE GEEMDRLTAS RERLGPVNLV AADELAEAEQ EHGSGLAEQE
ELAEAVNRLR GSIGALNREG RERLRAAFEA VDTHFQSLFT TLFGGGQAHL ALIDSDDPLE
AGLEIYAQPP GKKLQSLTLL SGGEQALTAV ALIFALFLTN PAPICVLDEV DAPLDDANIE
RFCDLLDAMI KQTETRYLIV THNAVTMSRM HRLFGVTMVE QGVSRLVSVD LGAAEDLLAA
E
//
