ID N9PV83_9GAMM Unreviewed; 1161 AA.
AC N9PV83;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, 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=F892_00798 {ECO:0000313|EMBL:ENX21566.1};
OS Acinetobacter vivianii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1776742 {ECO:0000313|EMBL:ENX21566.1, ECO:0000313|Proteomes:UP000013173};
RN [1] {ECO:0000313|EMBL:ENX21566.1, ECO:0000313|Proteomes:UP000013173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2168 {ECO:0000313|EMBL:ENX21566.1,
RC ECO:0000313|Proteomes:UP000013173};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 2168.";
RL Submitted (FEB-2013) 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}.
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:ENX21566.1}.
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DR EMBL; APRW01000009; ENX21566.1; -; Genomic_DNA.
DR RefSeq; WP_005256233.1; NZ_KB850134.1.
DR AlphaFoldDB; N9PV83; -.
DR PATRIC; fig|1217706.3.peg.761; -.
DR HOGENOM; CLU_001042_2_2_6; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000013173; Unassembled WGS sequence.
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; 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; 2.
DR PIRSF; PIRSF005719; SMC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|HAMAP-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 3..136
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT DOMAIN 392..1142
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 184..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 293..500
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 659..833
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 862..1005
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 1161 AA; 133352 MW; 4ED16708200C2FDE CRC64;
MRLSSLKLSG FKSFADSTTL NFKANRTAVV GPNGCGKSNV IDAIRWVMGE SNARQLRGGS
MQDVIFTGTA KRKPVGVASV ELRFDNTYGK LGGAYNAYNE LAVRRQVTRE GKSEYFLNGT
RCRRRDITDI FLGTGLGPRS YAVIEQGMIN RLVDAKPEEM RVFIEEAAGV SRYQARRRET
LQHLEHTEQN LARLDDIAAE LKSQLRSLKR QSEAAIQYKT LEGQIRTLKI EILSFQANQS
QKLQQEYTLE MTALGEQFKL VRSESQTIEH DLEATSALFQ RLIQQSSPLQ QEWQQAEKKL
AELKMTLEQK QSLFQQNSSS LVQLEQQKVQ TKERLQLSEL QIETLSAQFD EQNETLLALE
QQTQTAEQNV SDVQAQQKQA QQQFEQLKAQ VDKQQQQKLQ MAAQIEQLAK NVLRIEQQKQ
TLQSQSGQIR AQVQDEEQAQ LEQLQQQLHQ EIVELEAAIE ELQQNLQTQQ EQQQLDKADV
QTLKTEIQVL LAEQKNLNQL VAKQSPKHQQ NTLRLMQSLR LTAQGKSHAS IIEKFLAKWL
QAHLLDDEQS FQEGVARQLK NPSQPPFDKG RSSPLFQRGV RGDLKYLSDW IEAPQSSLWA
NVAVAESLAI ALAHQAELQQ TQSILTLDGY HVGADWVIGL HYDEDSQSAQ GMLSHQVRLE
EIELQLAEKQ PKLLELEQQF SQQQHTLQQQ QQQLQQQQQS LKQKQKELQQ LDVQIAKLQS
TAQAFVLQQQ QLADQLKQLD LQLEEDAMQR DDLEIDLHAL ALKLEAVLPN YKTLQFQVEN
LNEQLDEQQQ QLLQQQQQRE SLRRQTSQAN QQIELLEKDI SFLKTQYHQI IEQIEQAKKF
VDPIQLELPN LESQFQEQFH QTEKLQKNWN EWQLELNQIQ EKQQQLTEQR HQAQQKDEQV
REQLEQKRLA WQAAKSDREH YLEQLKELNA EALSDLSIEI KDHQQKLEKA QQQFEKIGAV
NLAASQEYEE VSQRFDELSH QMQDLQNTVD QLKDAMKSID QETRKLFMTT FDQVNQEMQV
LFPKVFNGGE ASLSLEDDWQ SGVKLMARPP GKRNSSLALL SGGEKTLTAL ALVFAIFRLN
PAPFCVLDEV DAPLDDANVQ RYCNLVKELS EQVQFIYITH NKLAMTMATD LLGVTMPEPG
TSKLVTVDLE QAKEYGLVAE S
//
