ID A0A255HNU3_9BURK Unreviewed; 1177 AA.
AC A0A255HNU3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:OYO29235.1};
GN ORFNames=CD932_19280 {ECO:0000313|EMBL:OYO29235.1};
OS Janthinobacterium sp. PC23-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=2012679 {ECO:0000313|EMBL:OYO29235.1, ECO:0000313|Proteomes:UP000216749};
RN [1] {ECO:0000313|EMBL:OYO29235.1, ECO:0000313|Proteomes:UP000216749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC23-8 {ECO:0000313|EMBL:OYO29235.1,
RC ECO:0000313|Proteomes:UP000216749};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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}.
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:OYO29235.1}.
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DR EMBL; NJGY01000002; OYO29235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255HNU3; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000216749; 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; 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}.
FT DOMAIN 518..628
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 170..278
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 314..369
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 458..506
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 697..724
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 760..904
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 981..1018
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 1177 AA; 132021 MW; BBD20421E87EFBEF CRC64;
MRLSSIKLSG FKSFVDPTNF QVPGQLVGVV GPNGCGKSNI IDAVRWVLGE SKASELRGES
MQDVIFNGST HRKPAGRASV ELVFDNNDGK ASGQWGQYAE IAVKRTLTRD GTSTYYINSQ
PVRRRDIQDI FLGTGLGPRA YAIIGQGMIS RIIESRPEEL RVFLEEAAGV SKYKERRRET
ENRLQDTREN LLRVEDILRE LNANLEKLEA QAAVATRFHA LQADQEEKQK LLWLLRKNEA
QNEQTRYFRE VEQAQTDLEE QAAKLRNVEL TLEQMRQAHF AVGDRLHTAQ GHLYQTNAEI
GSLEAQIKFV IESRARLQAQ LATLTAQRDQ WSGQGGEYQE QLEEAEFQLE ELAAKVEQSQ
MMAEQKGEQL PELDAAWRAA QHKSTESRAK IMQAQQQLEL ESAHQRNASN ILNSLLSRRE
RLQQEKNSLS LPDSSHLDNL KLQLEEKQQT LEEQGFYLEE ALEQQPRLEQ ERSEAQAQVN
AETNANAQLE ARLSALKQLQ ERVQTQGKVQ PWLKKHELDT LPRLWQKLQI EAGWEAAMES
ILRERTSALQ LSNIDWAKAF FADAPPAKLA LYAPSTVPPL PLPLLEVPGL KPFINLLKLN
DPGLRGLLQD WLHNAYAVED AAEALAERGK LPPGGYFVTR AGHVVTAGSV RFYAADSEQE
GMLGRQQEID NIGKQLRAQQ LLAEEARARS VRADAAVAAS SRNLSDLRLR MQQLTAAVHG
LQLDVVKLSE VEARFNQRST QIGTDLAEIA AQEAEQQQIK MESEEKFEQL DMALGTLQEE
HEDGQTDFLR KEQRLSEARD ALRDLERAAK DTEYAEKSQR TRIEELRRNI ATASTQAQQV
TASLQAGQLE LANLESGAAN DGLQDLLERR TTQEKALADA RHELDQITQQ LRLLEDARAQ
SERSLQPQRD KIMEMQLKEQ AARLNQEQFA QQLLESGADE AALTEKLHPD MRPSYLQGEV
TRLTNAIAAL GAVNLAALDE LAQASERKNF LDAQNADLTE AINTLEDAIH KIDKETRDLL
QDTFDKVNHH FSELFPILFG GGQARLTMTG DEILDSGVQV MAQPPGKKNA TIHLLSGGEK
ALTATALVFS MFRLNPAPFC LLDEVDAPLD DSNTERFCRM VKRMSDQTQF LFISHNKIAM
EMAHQLIGVT MQEQGVSRIV AVDMESAANF ATEAQAA
//
