ID L1NUA2_9NEIS Unreviewed; 445 AA.
AC L1NUA2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=HMPREF9120_01214 {ECO:0000313|EMBL:EKY06988.1};
OS Neisseria sp. oral taxon 020 str. F0370.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1127694 {ECO:0000313|EMBL:EKY06988.1, ECO:0000313|Proteomes:UP000010457};
RN [1] {ECO:0000313|EMBL:EKY06988.1, ECO:0000313|Proteomes:UP000010457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0370 {ECO:0000313|EMBL:EKY06988.1,
RC ECO:0000313|Proteomes:UP000010457};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU362031};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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:EKY06988.1}.
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DR EMBL; AMER01000097; EKY06988.1; -; Genomic_DNA.
DR RefSeq; WP_009425634.1; NZ_KB291094.1.
DR AlphaFoldDB; L1NUA2; -.
DR STRING; 1127694.HMPREF9120_01214; -.
DR PATRIC; fig|1127694.3.peg.1130; -.
DR HOGENOM; CLU_025778_0_2_4; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000010457; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd00989; PDZ_metalloprotease; 2.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF17820; PDZ_6; 2.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR PROSITE; PS50106; PDZ; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW Metal-binding {ECO:0000256|RuleBase:RU362031};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU362031};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EKY06988.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010457};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362031};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 419..437
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 111..181
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 218..272
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 445 AA; 47770 MW; 580F6B4EE9AEB718 CRC64;
MLTLVSFIVA ILILVSLHEL GHLLVARLCG IKVLRFSVGF GKPFFTKRWR NIEWCFAPIP
LGGYVKMVDT REGNVAEADL PYAFDKQHPA KKIAVVAAGP LTNLALAVLL YGLSFSFGIS
ELKPFVGTVE PYSIAAKAGF AAGDKITAVN GVPVANWGDA QTGIVLDLEA GKVDVAVTTE
QGRNIVRTID AAGTQEAADV AKRGGYIGLM PYKLTKTVSV VVPGSAAEKA GLKAGDTLLA
ADGKALGDWQ EWVDLVRRSA GQKLQLTYLR DGKTLQTFIR PDSEMQGGVL SGRVGLGAAT
DKVWDKAVRF RYYPSVAEAF GMAWRKTTGY VTLTLKFFGR LLGGQASLQH VSGPLTIADV
AGKSASMGWQ PYVEFLALVS VSLGVMNLLP VPVLDGGHLV FYSIEWLRGK PLSESIQTAG
LRVGLALMMM LMILAFFNDI TRLFG
//
