ID U2E4A5_9GAMM Unreviewed; 1170 AA.
AC U2E4A5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:ERJ18681.1};
GN ORFNames=SSPSH_002389 {ECO:0000313|EMBL:ERJ18681.1};
OS Salinisphaera shabanensis E1L3A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ18681.1, ECO:0000313|Proteomes:UP000006242};
RN [1] {ECO:0000313|EMBL:ERJ18681.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18681.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=21705588; DOI=10.1128/JB.05459-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium from
RT the harsh, variable environment of the brine-seawater interface of the
RT Shaban Deep in the Red Sea.";
RL J. Bacteriol. 193:4555-4556(2011).
RN [2] {ECO:0000313|EMBL:ERJ18681.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18681.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERJ18681.1}.
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DR EMBL; AFNV02000016; ERJ18681.1; -; Genomic_DNA.
DR RefSeq; WP_006913474.1; NZ_AFNV02000016.1.
DR AlphaFoldDB; U2E4A5; -.
DR STRING; 1033802.SSPSH_002389; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000006242; 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; 1.10.287.1490; -; 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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000006242}.
FT DOMAIN 3..1155
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 370..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 171..212
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 372..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..890
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 1170 AA; 129358 MW; 6E189DBF83FB65C7 CRC64;
MRLTSIRLAG FKSFVDPATL ALNSNLTGVV GPNGCGKSNV IDAVRWVTGE SSARQLRGEA
LEDVIFNGSK ARKPVGRASV ELKFDNSDAT LTGQYGAFSE ISVKRELSRD GGSRYYINGT
KSRRRDVIDL FLGTGLGGRS NYAVIEQGAV NRLIEAKPED MRQVLEEAAG ISKYKERRRE
TENRMRHTRE NLDRLNDLIG EVTQRLGVLK RQAANAEKYK QFKAEERRLR AELLALRWAA
ENEKVEVAEG RLRASEHELR EAISTQRSAQ QARAAEAESQ QKAMGAVQTQ QAAFYDAQAQ
ASRIAQALAH AKEMRELRER ERDELVERRD ALAKRIAEDE HAEHDTVSAA EAIATEHDEA
QRALTQAREA LDGAEKAARE AESAWDAHNS AEQNPVQQLD AERRRARYAE ERVQQLGARR
DKRRGERDKL DDEDTGDLAA GARDIESRAG QLAEDEKTAA NQAESDDALR AAINDAEADV
EARRTQLGET RARLASERQL QQSVLREDDA TLAQWLADNA QTEAAGVARR VKVRGPWQTA
AEAVLGPWLR GFVVERLPAL AGDWPSESLT LVESGPADPV GAARGPADTP SLAEGIEAPA
VIAALAARVF VVDDLAAALE YRHELTEDQR FVTLDGCCIG PHSLVTPAAG SAEQGVLERE
QRIETLAVQI DAEQAELDSL QETLDGQREQ RDERREQRRA LEQRIAQARR ELEAARAEQQ
GREIRAEQLA RRRKELDNEL ADLENQITEA AGEFERLSAQ VTALEDKAEA FSAARREAQA
QLAESRAARD AARKAYAQAE RALREIETRS EQNRSRAESI AQRLADTRDA RSDVETRLAG
FDDDSAASDK EATPAPDESE HEQALEAQHR AERELRAARE SLKASEKALD EASQRQMQAE
QGVETAREGL QQAKIDVETT RVRRAGIAEQ IEELGETPAA LVANLEDGAT IETRTAAIET
IERKIQRLGA INLAAIEEYD AEAERERYLG EQHADLSEAL ETLETAIARI DRETRARFKA
TYEQVNERFA GMFPELFGGG EAALELTEDD WLVTGIRVMA RPPGKRNASI QMLSGGEKAL
TAVALLFALF ELNPAPFCML DEIDAPLDDA NVSRFCELVR RMSAQVQFIV ITHNKLTMSL
AEQLHGVTMA EPGVSRLVSV DIDQALDMAG
//
