ID Q5F9I3_NEIG1 Unreviewed; 443 AA.
AC Q5F9I3;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Peptidase PmbA {ECO:0000313|EMBL:AAW89154.1};
GN Name=pmbA {ECO:0000313|EMBL:AAW89154.1};
GN Synonyms=tldE {ECO:0000313|EMBL:AAW89154.1};
GN ORFNames=NGO_0411 {ECO:0000313|EMBL:AAW89154.1};
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89154.1, ECO:0000313|Proteomes:UP000000535};
RN [1] {ECO:0000313|Proteomes:UP000000535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535};
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase U62 family.
CC {ECO:0000256|ARBA:ARBA00005836}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004969; AAW89154.1; -; Genomic_DNA.
DR RefSeq; WP_003687847.1; NC_002946.2.
DR RefSeq; YP_207566.1; NC_002946.2.
DR AlphaFoldDB; Q5F9I3; -.
DR STRING; 242231.NGO_0411; -.
DR KEGG; ngo:NGO_0411; -.
DR PATRIC; fig|242231.10.peg.494; -.
DR HOGENOM; CLU_026425_0_0_4; -.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.2290.10; PmbA/TldD superfamily; 1.
DR InterPro; IPR045569; Metalloprtase-TldD/E_C.
DR InterPro; IPR045570; Metalloprtase-TldD/E_cen_dom.
DR InterPro; IPR002510; Metalloprtase-TldD/E_N.
DR InterPro; IPR047657; PmbA.
DR InterPro; IPR035068; TldD/PmbA_N.
DR InterPro; IPR036059; TldD/PmbA_sf.
DR PANTHER; PTHR43421; METALLOPROTEASE PMBA; 1.
DR PANTHER; PTHR43421:SF1; METALLOPROTEASE PMBA; 1.
DR Pfam; PF01523; PmbA_TldD_1st; 1.
DR Pfam; PF19290; PmbA_TldD_2nd; 1.
DR Pfam; PF19289; PmbA_TldD_3rd; 1.
DR SUPFAM; SSF111283; Putative modulator of DNA gyrase, PmbA/TldD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000535}.
FT DOMAIN 29..93
FT /note="Metalloprotease TldD/E N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01523"
FT DOMAIN 121..227
FT /note="Metalloprotease TldD/E central"
FT /evidence="ECO:0000259|Pfam:PF19290"
FT DOMAIN 234..442
FT /note="Metalloprotease TldD/E C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19289"
SQ SEQUENCE 443 AA; 47796 MW; 780EADFED348DA48 CRC64;
MLFNHTASEL LDLCRRTLDL AKAAGATAAE ADFSESLGQS VSVRLGEIEQ IEFQQDKSLD
ITVYVGKRKG RAGTADFSEQ ALRDTVRAAA DIARHTAEDG CAGLADPELM AQHIGDPDLY
HEWDLDTEAA VGLAKQCEQA ALDTDSRIEN SEGAAVQTGH YQYVYGNTHG FAAHRQSTHH
SISCSVVAAD ENGMQRDYWY DSACRHPDMD SPETIGQTAA RRTLRRLGSR SIPTGSYPVL
FDTTVSGGLI GHLVGTLSGG ALYRQSSFLI DSIGKKVLPD FLNLREEPHI PRSFRSSYFD
AEGVATAPRF VIQNGIVEGY FLGSYSARKL GMQTTGNAGG AHNLYLNHTH ETQSDLLKEM
GTGLLVTELM GQGANTITGD YSRGAAGFWV ENGVIAYPVH EITVAGRLQD MYRDIVGVAD
DALRRSSNKI GSILIAGMTV AGS
//