ID W6KEB3_MAGSQ Unreviewed; 458 AA.
AC W6KEB3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Putative Peptidase M23B {ECO:0000313|EMBL:CCQ75673.1};
GN ORFNames=MGMAQ_3868 {ECO:0000313|EMBL:CCQ75673.1};
OS Magnetospira sp. (strain QH-2) (Marine magnetic spirillum (strain QH-2)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Magnetospira.
OX NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ75673.1, ECO:0000313|Proteomes:UP000032733};
RN [1] {ECO:0000313|EMBL:CCQ75673.1, ECO:0000313|Proteomes:UP000032733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-2 {ECO:0000313|EMBL:CCQ75673.1,
RC ECO:0000313|Proteomes:UP000032733};
RX PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N., Murat D.,
RA Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S., Pradel N.,
RA Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B., Coutinho P.M.,
RA Li Y., Xiao T., Medigue C., Barbe V., Pignol D., Talla E., Wu L.F.;
RT "Comparative genomic analysis provides insights into the evolution and
RT niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL Environ. Microbiol. 16:525-544(2014).
CC -!- SIMILARITY: Belongs to the LECT2/MIM-1 family.
CC {ECO:0000256|ARBA:ARBA00024361}.
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DR EMBL; FO538765; CCQ75673.1; -; Genomic_DNA.
DR RefSeq; WP_052716545.1; NZ_FO538765.1.
DR AlphaFoldDB; W6KEB3; -.
DR STRING; 1288970.MGMAQ_3868; -.
DR KEGG; magq:MGMAQ_3868; -.
DR HOGENOM; CLU_596908_0_0_5; -.
DR OrthoDB; 9810477at2; -.
DR Proteomes; UP000032733; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR008663; LECT2.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR11329; LEUKOCYTE CELL-DERIVED CHEMOTAXIN 2; 1.
DR PANTHER; PTHR11329:SF0; LEUKOCYTE CELL-DERIVED CHEMOTAXIN-2; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032733};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 328..426
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT REGION 153..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 50364 MW; FE3796C032FBBC8F CRC64;
MPEDTWDGMA PPKPGEIRAI RAKSVAERTH ADQRRLHWAE DYWTNEDIQT ETTAFYKLNS
EVGAPTGHAT GHAPFGADSA RTEDAKINRQ RADHAIKSLG PDADPDHVRL VEAHYGVGEP
AQAISMDEQG NWYDAQGNIF DQDRRYEKTI DSTQDAQHHQ EWGSVSEWDN RNDSKHSQPV
LREFEIAKNP GHWDGKPNGR VENFQGLENR RPDMVVSHQG HFFESRAYGS QRLQALDSHN
SLQQAPHTQD QGGFQLANAT GSQAGIKGNF MQPTASQVAQ AGNQQSPSQA SNRKPPQLAS
PVPGGAIRSP DAMGDGRYGA SRDGGKRNHQ GVDIVANPGQ DVTSTVDGTV TKLGYPYAND
KSYRYVEIQT KDGYVVRHFY VNPGNLKPGQ AVVAGKTKIG TVQDLSKRYP KGMTNHIHVE
IRDRNKVAYP NKSGSRKFQD LDPTSLLQAP GPQGGGTP
//
