ID A9LZE1_NEIM0 Unreviewed; 436 AA.
AC A9LZE1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Replication-associated recombination protein A {ECO:0000256|ARBA:ARBA00020776};
GN OrderedLocusNames=NMCC_1143 {ECO:0000313|EMBL:ABX73317.1};
OS Neisseria meningitidis serogroup C (strain 053442).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=374833 {ECO:0000313|EMBL:ABX73317.1, ECO:0000313|Proteomes:UP000001177};
RN [1] {ECO:0000313|EMBL:ABX73317.1, ECO:0000313|Proteomes:UP000001177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=053442 {ECO:0000313|EMBL:ABX73317.1,
RC ECO:0000313|Proteomes:UP000001177};
RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA Liang X., Xu J., Jin Q.;
RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT clone.";
RL Genomics 91:78-87(2008).
CC -!- FUNCTION: DNA-dependent ATPase that plays important roles in cellular
CC responses to stalled DNA replication processes.
CC {ECO:0000256|ARBA:ARBA00002393}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00008959}.
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DR EMBL; CP000381; ABX73317.1; -; Genomic_DNA.
DR RefSeq; WP_012221690.1; NC_010120.1.
DR AlphaFoldDB; A9LZE1; -.
DR KEGG; nmn:NMCC_1143; -.
DR HOGENOM; CLU_017985_1_1_4; -.
DR Proteomes; UP000001177; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 46..162
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 436 AA; 48321 MW; B5CA52C2B833DA9F CRC64;
MTDLFAREPD APLAERLRPH TLDDVVGQEH LIGEGKPLRV AVEGGKPHSM LLWGPPGVGK
TTLARILAQS FNAQFLPVSA VFSGVKDIRE AIDKAEIALQ QGRATILFVD EVHRFNKAQQ
DAFLPHVESG LLTFIGATTE NPSFEVNPAL LSRAQVYVLQ PLSSDGLKKL VAKVLALPEY
RDFTIEADAQ ELFVNTADGD ARRLLNLLEQ LLRAADTRRL KNLTAEFLAD SLGAQIRRFD
KGGESFYNQI SALHKSVRGS HPNAALYWFC RMLDGGTDPR YLARRIVRIA WEDIGLADPR
AFQIANDAAA TFERLGSPEG ELALAQAVLY LAAAAKSNAG YKAYNQMRHF VKENASDEVP
VHLRNAPTKL MKELGYGREY RYAHDEPNAY SAGESYMPDG LDEPDFYQPV PRGLEIKIGE
KLAWLKSLDE EALKAK
//
