Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P37609

Entry ID Method Resolution Chain Position Source
AF-P37609-F1 Predicted AlphaFoldDB

No variants for P37609

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P37609

No associated diseases with P37609

1 regional properties for P37609

Type Name Position InterPro Accession
domain Lantibiotic biosynthesis protein, dehydration domain 87 - 460 IPR025410

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

1 GO annotations of biological process

Name Definition
bacteriocin biosynthetic process The chemical reactions and pathways resulting in the formation of a bacteriocin, any of a heterogeneous group of polypeptide antibiotics that are secreted by certain bacterial strains and are able to kill cells of other susceptible (frequently related) strains after adsorption at specific receptors on the cell surface. They include the colicins, and their mechanisms of action vary.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKKKTYQFEK FLKNTFDQFS IKQNEVLVED DLNDIIMNVC GKALVLMINE KREMNLLMGN
70 80 90 100 110 120
TPEERYQYFE NEYSSTGKAF EEIKDKFPVI YIDLKNSINS YLKLVSQIMK DFKKDYSLLV
130 140 150 160 170 180
ERKIIEEHST ISTMKIKGDL HNGKAVIEIT TNKSKLIYKP KSLSNDVFFN NFLKYMDSFF
190 200 210 220 230 240
IKEGKSTKYK ENFYLVNTLD MKTYGWVEYV DKKPINSFEE ARNYYRKIGV LLSVAYTLNL
250 260 270 280 290 300
TDLHFENVIS QGENPCIIDL ETMFNMPMFV KDYKNESRNI INGKIMDSVV STGMLPVLGI
310 320 330 340 350 360
DSLFGGDPSG ILGGTFSKEE RVIINPFRDD IKFQKIVVRS VFKDHIPFFN NNNEKRYCKP
370 380 390 400 410 420
KDYVNDIIKG FEKTYKIIVK NKEKILGFLK KESSSVTCRI LFRNTMEYSV LLNAAKSPVY
430 440 450 460 470 480
SNKREEIFEK LSTFNRGLGN DIIKSEISQI NTLSIPYFNC QVDSNLIKNM DGETIFEHTL
490 500 510 520 530 540
TPFKCFLSKY RRLCVDDMEQ QVKLIRFSIQ SQEQLFKDGE QFSLYKKQKG SQEDLLIAIN
550 560 570 580 590 600
ELSSILENNA YIGTSDDTIN WMSLGIADND QILFESLEND IYKGISGIGL ALLEYYEFYP
610 620 630 640 650 660
NINTKKILKL IYKNISKDFI NTNNEPQNYG FYVGLIGEYS FLRKYEKVFH KTSSCNILKN
670 680 690 700 710 720
ILKDFTPEKC QTILPSDDVI AGEAGIIIYI SNLNNYLEYR DEIDILLKSL SNKIKLKESI
730 740 750 760 770 780
ASYAHGNSGI ATAFVHGYKV TKNEKYLKIF HELWNLENSS KLRRGWTDSR KVDSSYSSQW
790 800 810 820 830 840
CHGASGQAIA RMEWITVNKT ARFLSNSELI KVKKELGELI DILKKEGMYT DNFCLCHGIL
850 860 870 880 890 900
GNLLILNTYQ ENFDNKNINL KNEILNNYYS VCNYGLNKGW ICGLGTEFYS YGLMTGISGI
910 920
LYGLIRQVKQ KNNFGVLMPY VD