ID A0A0B4XHR5_9GAMM Unreviewed; 1164 AA.
AC A0A0B4XHR5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=S7S_06490 {ECO:0000313|EMBL:AJD47714.1};
OS Isoalcanivorax pacificus W11-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Isoalcanivorax.
OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD47714.1, ECO:0000313|Proteomes:UP000006764};
RN [1] {ECO:0000313|EMBL:AJD47714.1, ECO:0000313|Proteomes:UP000006764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD47714.1,
RC ECO:0000313|Proteomes:UP000006764};
RX PubMed=23209202; DOI=10.1128/JB.01845-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT type strain W11-5, isolated from deep sea sediment.";
RL J. Bacteriol. 194:6936-6936(2012).
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; CP004387; AJD47714.1; -; Genomic_DNA.
DR RefSeq; WP_008739012.1; NZ_CP004387.1.
DR AlphaFoldDB; A0A0B4XHR5; -.
DR STRING; 391936.S7S_06490; -.
DR KEGG; apac:S7S_06490; -.
DR HOGENOM; CLU_001042_2_2_6; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000006764; 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; 2.
DR Gene3D; 1.10.287.1490; -; 2.
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 SMART; SM00968; SMC_hinge; 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:UP000006764}.
FT DOMAIN 520..617
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 444..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..264
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 868..902
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 979..1009
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 444..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..797
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 1164 AA; 132920 MW; 399CE71CBFA617D2 CRC64;
MRLKSIKLAG FKSFVDPTTA LFPENLTAVV GPNGCGKSNI IDAVRWVMGE SSAKHLRGES
MADVIFNGSN ARKPVAQASI ELVFDNGDGK IGGEYARYAE ISVRRMVTRD GQSNYFLNGT
KCRRKDITDL FLGTGLGARS YAIIEQGMIS RLIEARPEDL RVYIEEAAGI SRYKERRRET
ENRMRRTREN LERLTDIREE LERQLERLSR QAAAAEKYKQ YKEEERLVGA QVRALRWRTL
NTQVEQIEHV MRELEVAVEA KVAEQRHVDA ELERLRDGHT DVQDRFNSVQ QEYYALGAEV
ARLEQSIQHQ RERKQQLNEE LMQVEQNWRE ASAHLSTDGE RIAELDEKLA ELEPELALVR
EQEAEAVEQL AMAEEQMQTW QQEWETFNHS SAESRRKAEV EQSRIQHLET SIERLSDRID
RLSKEQGSLD AGPLSAEMRQ FEEQQAQLRE QAEEAEMRSE SVQEQINSIR RDNGERGRQL
DEDRDQLQKM KSRHATLEAL QKAAQGDDGR VSEWFERHQL QQRPRLAEKL DVQPGWERAV
EAVLGDSLQG LCVEGFDQVE QWLGDLSHGR VCLLAPSNAA KDGAHGRTLA ALVSGPVPAQ
LGQIYAVESL ADALALRGRL SAAESAVTRD GIWVGPDWLR VVREQDQEAG ILERRRELER
LEDQIPELDA RVAENRAALE AGRERVQELE HEREESQRQA SRINRDLGEL NAQISARQVR
LEQITMRRER LGRELDESRE QRTQEQEQLK EARSVLTEAL DAMEQDSGQR EALLSRRDSA
RSQLDEARQK ARQQRDQSHQ LAMEVQGART QADSLRQGLV RLDAQVASLT ERKALLERQL
DEGDDPGIEL KAQLEEKLGL RLESETRLQS VRRELETIDH EVRNLDGQRQ QFERQAQEVR
SALDGKRMQW QEIKVRRSTV QEQLAEQQFD LQTVLENLPE DAAEDTWNQE LEAIAARISR
LGQINLAAID EYKTQAERKE YLDRQNADLD DALNTLENAI RKIDRETRTR FKEYFDRINK
GLQELFPKVF GGGHAYLELT GEDLLDTGVA IMARPPGKRN STIHLLSGGE KALTALSLVF
SIFQLNPAPF CMLDEVDAPL DDANVGRFCN LVREMSGVVQ FIYITHNKIA MEMAHALMGV
TMHEPGVSRL VSVDVDEAAE MAAL
//