ID A0A286GVX8_9PROT Unreviewed; 1162 AA.
AC A0A286GVX8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=SAMN05421508_109125 {ECO:0000313|EMBL:SOD99683.1};
OS Caenispirillum bisanense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD99683.1, ECO:0000313|Proteomes:UP000219621};
RN [1] {ECO:0000313|EMBL:SOD99683.1, ECO:0000313|Proteomes:UP000219621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 140 {ECO:0000313|EMBL:SOD99683.1,
RC ECO:0000313|Proteomes:UP000219621};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; OCNJ01000009; SOD99683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286GVX8; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000219621; Unassembled WGS sequence.
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; 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; 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; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000219621}.
FT DOMAIN 5..1146
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 416..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 178..212
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 810..893
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 957..998
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1162 AA; 128025 MW; 1C176DC125F0E82F CRC64;
MIRFSRLRLS GFKSFVDPTD LLIEPGMTGV VGPNGCGKSN LVEALRWVMG ETSAKQMRGG
EMDDVIFGGT ATRPSRNIAE VTVSLDNRDR SAPALFNTVD ELEITRRIER GKGSVYRVNG
KETRAKDVML LFADAATGAR STAMVSQGRV GALINAKPSQ RRSLLEEAAG IGGLHTRRHE
AELRLKGAEA NLQRLEDVLQ ALGAQLGNLR KQARQAARYR ALSEQIRQVE ALVLHLRWTK
AITALEKAKE QFRLAEGRVA ELTGLAASAS RAHLEADEAM PALRQAEAEA AARLQRLVLA
REQLDAEERR IASARQDAEV RLRQIADDID RERLRAQDAD EAVARLEEER DALIEASSDE
ELEQEEARER LQRVNDDVTE REAELTRLTE RAAAEDAQRK ALLRRAEEAD LRAERAERRL
RETEDSRASA AAAGVPREDL DVAEERLYAA EEALETARAA RAAAEEARDA RQGDYEAARD
ALQTESAARA RLKAEIDALT DLLAGDRDET TGEATAPVLD ALAVRPGSEQ ALGAALGDDL
AAPVAETGAR RWQALPPVAG AAGLPAGVEP LDRMVSGAPA LARRLAATGL VKDRDTAAAL
ARELAPGQRL VTPEGDLWRW DGFVAEAGAP SAAATRLKQR NRLAELRESL VELDERVEVA
ETRVEDARLA VEHAQEAART ARDRERAAEQ SLTDARNRQI ELSRRNAATE SRLSALDQTL
EQLAADLAEA RAQVEEAREQ RARLGDGGGD RQRVDTLRAE VAELRTRLAE ARSLHDRVFR
EAEERARRVK AVEAELESWH RRKDGTAGQF EELEARREAV MEDLAHLAER PVEIAEQRET
LAEEIERAEV QRRIAADRLA EGDSRLRDAD RTLREAEQAL AKAREERVRG EGAVETGRQQ
CQQIAAAIAE RLDCTPEQTR ALAGLDDPEA PAAPDLGEAE DRLQRLSRER EMMGPVNLRA
EQEAQELEEQ VATLTAERDD LTGAIARLRQ GIAELNREGR QRLLASFEKV DRNFRTLFVR
LFGGGRAHLA LTESDDPLEA GLEIMASPPG KRLQILSLLS GGEQAMTALA LLFAVFLVNP
APICVLDEVD APLDDANVDR FCAMLDELTR MSEASTRFLV VTHHRMTMAR MDRLFGVTMA
ERGVSTLVSV DLHEAERLRE AG
//
