ID A0A0W7YUG4_9BURK Unreviewed; 1174 AA.
AC A0A0W7YUG4; A0A1V0BHA6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=AS359_07765 {ECO:0000313|EMBL:KUF38780.1}, B5M06_14145
GN {ECO:0000313|EMBL:AQZ99224.1};
OS Comamonas kerstersii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=225992 {ECO:0000313|EMBL:KUF38780.1, ECO:0000313|Proteomes:UP000053300};
RN [1] {ECO:0000313|EMBL:KUF38780.1, ECO:0000313|Proteomes:UP000053300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12322-1 {ECO:0000313|EMBL:KUF38780.1,
RC ECO:0000313|Proteomes:UP000053300};
RA Ming D., Wang M., Hu S., Zhou Y., Jiang T.;
RT "Complete genome sequence of a multi-drug resistant strain Acidovorax sp.
RT 12322-1.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AQZ99224.1, ECO:0000313|Proteomes:UP000242792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8943 {ECO:0000313|EMBL:AQZ99224.1,
RC ECO:0000313|Proteomes:UP000242792};
RA Zheng B.;
RT "Rapid Whole Genome Sequencing of Comamonas kerstersii Causing Continuous
RT ambulatory Peritoneal Dialysis-Associated Peritonitis.";
RL Submitted (MAR-2017) 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. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; CP020121; AQZ99224.1; -; Genomic_DNA.
DR EMBL; LPXH01000038; KUF38780.1; -; Genomic_DNA.
DR RefSeq; WP_054067092.1; NZ_LPXH01000038.1.
DR AlphaFoldDB; A0A0W7YUG4; -.
DR STRING; 225992.B5M06_14145; -.
DR GeneID; 83040455; -.
DR KEGG; cke:B5M06_14145; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000053300; Unassembled WGS sequence.
DR Proteomes; UP000242792; 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; 1.
DR Gene3D; 1.20.5.170; -; 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; 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 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:UP000053300}.
FT DOMAIN 3..1158
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT DOMAIN 524..626
FT /note="SMC hinge"
FT /evidence="ECO:0000259|Pfam:PF06470"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 255..499
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 683..904
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 1174 AA; 130735 MW; 5FC47366B646CAD6 CRC64;
MRLNSIKLSG FKSFAEPTNF MLPGQLIGVV GPNGCGKSNI MDAVRWVLGE SKASELRGES
MQDVIFNGTT HRKPASRSSV ELVFDNSDHR AGGQWGQFTE IAVKRVLTRD GNSSYFINNQ
PVRRRDVQDV FLGTGLGPRA YAIIGQGTIS RIIESRPEEL RLFLEEAAGV SKYKERRRET
ENRLSDTREN LTRVEDILRE LNANLDKLEK QAEVAARYNE LQASVTLKQH QLWFLKKQDA
EGDLTKIRQE GLQAVNELEA RMAEIRHIEA DLEAVRQAHY EAGDKVNQAQ GRLYEATAEV
GKLEAEIRYV VEGRQRVEQR LQQLAEQIAQ WAQRKEDAEV ELEHLAENGM DAEEQAEMLA
AQLEEQSMRL PDLEDALRAA QNKANEQRQQ VVQVQQQIQV LAAEQRSINE QTRQHESRLE
RLRNDRNALA TPDEARLQQV SAQYEDAAEM AEMAEAALME LQDSVPQLDD ERRQRQQALN
QETARQAELA ARMEALKALQ EKVKTDGKLQ PWLAKHGLDG LQGLWTRIAV EPGWENALEA
ALRERMGALE ISRLDMVRGF LGAGAKDAPP ARLAFYSKPE GSLSLSSNGL PLMAELLRVG
DAGLKALLTE WLAGCYTAQS LDEALSHRAQ LKAGETIYVP TGHAVTAHSV SFFAQDSEQS
GLLARAQEIE HLEKELRAQA LISEEARTAL VRAEAAYADA SQRLVSARRE ASEAKQSAHE
LQVEMLRLTQ QAEQARARTA QIEADVAEVQ AALDDLQERA VAAEARFEEL DMQLADSQEL
HAQLDEKVIE AERKLAESRE QLRALERKAQ EATFSQRSMQ ARQAELQRTL ETAEQQTKAL
LEERERAYAE QSRLNDAAAQ GGLQDALALK MEREQAVAAA RSEYEDLTNK LRASDERRTQ
IERALEPMRA RITEFQLKEQ AAALGSAQYE QQLAEAGADL AAVAQSILEG NVKLHGLQSE
IDRLHREIAA LGAVNLAALE ELQLARERKV FLDAQVADLT EAMTTLENAI KKIDNETRDL
LSATFNTVNT HFGRMFPELF GGGQAKLIMT GDEILDAGVQ VMAQPPGKKN QTIHLLSGGE
KALTAIALVF AIFQLNPAPF CLLDEVDAPL DDANTERYAK LVASMSRGTQ FLFISHNKIA
MEMAQQLIGV TMQEQGVSRI VAVDMESALS MAHA
//
