ID G7Z2N4_AZOL4 Unreviewed; 456 AA.
AC G7Z2N4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Putative Zn-dependent protease {ECO:0000313|EMBL:CBS87658.1};
GN OrderedLocusNames=AZOLI_2452 {ECO:0000313|EMBL:CBS87658.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS87658.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
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DR EMBL; FQ311868; CBS87658.1; -; Genomic_DNA.
DR AlphaFoldDB; G7Z2N4; -.
DR STRING; 862719.AZOLI_2452; -.
DR KEGG; ali:AZOLI_2452; -.
DR HOGENOM; CLU_030556_2_0_5; -.
DR Proteomes; UP000005667; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07324; M48C_Oma1-like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CBS87658.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..456
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003506846"
FT DOMAIN 47..233
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 433..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 49013 MW; A39190EA7102F34C CRC64;
MRKPSRLVSV VAIMSMCLMS LVWGAPPASA QRRSDMQILG DAETDHIIRK MARPIFQAAG
IDPESVQILL VNDPSVNAFV AGGQNIFLHT GLLLNVDDAD QLLGVIAHET GHISGGHLVR
GAEAMDNAFL SSLLGMGLGV IGGLASGNAG AGAAGVMLGQ HLAERNFLSF SRTQEASADQ
AGLSFLEQSG ISARGMAAFL EKLGVGEPLM NDRDAGYRLT HPLTRERIEA VKAFVARSRY
ADARLPAATE SDLRRLQAKL YGYLDPRGAL QRYKANDPSP AARYGRAYAY FRQGDVRQAT
PLVDGLIADE PRNPYLHEMK GDLMLQTGRA PDAVAPYRKA IELAGSEAGT IRVSLAHALL
EQRDPRLADE ALKNLQIAAK GKAQSAFLWR LTAQAWSMKK NDGMVAYATA EEALARGDMP
MAKAQAERAE KLLPAGSPGW LRAQDIRGQT GGDRPR
//
